TY  - JOUR
AU  - Cenni, Vittoria
AU  - Kojić, Snežana
AU  - Capanni, Cristina
AU  - Faulkner, Georgine
AU  - Lattanzi, Giovanna
PY  - 2019
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1282
AB  - Ankrd2 (ankyrin repeats containing domain 2) or Arpp (ankyrin repeat, PEST sequence, and proline-rich region) is a member of the muscle ankyrin repeat protein family. Ankrd2 is mostly expressed in skeletal muscle, where it plays an intriguing role in the transcriptional response to stress induced by mechanical stimulation as well as by cellular reactive oxygen species. Our studies in myoblasts from Emery-Dreifuss muscular dystrophy 2, a LMNA-linked disease affecting skeletal and cardiac muscles, demonstrated that Ankrd2 is a lamin A-binding protein and that mutated lamins found in Emery-Dreifuss muscular dystrophy change the dynamics of Ankrd2 nuclear import, thus affecting oxidative stress response. In this review, besides describing the latest advances related to Ankrd2 studies, including novel discoveries on Ankrd2 isoform-specific functions, we report the main findings on the relationship of Ankrd2 with A-type lamins and discuss known and potential mechanisms involving defective Ankrd2-lamin A interplay in the pathogenesis of muscular laminopathies.
PB  - Hindawi Ltd, London
T2  - Oxidative Medicine and Cellular Longevity
T1  - Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies
VL  - 2019
DO  - 10.1155/2019/7318796
ER  - 

@article{
author = "Cenni, Vittoria and Kojić, Snežana and Capanni, Cristina and Faulkner, Georgine and Lattanzi, Giovanna",
year = "2019",
abstract = "Ankrd2 (ankyrin repeats containing domain 2) or Arpp (ankyrin repeat, PEST sequence, and proline-rich region) is a member of the muscle ankyrin repeat protein family. Ankrd2 is mostly expressed in skeletal muscle, where it plays an intriguing role in the transcriptional response to stress induced by mechanical stimulation as well as by cellular reactive oxygen species. Our studies in myoblasts from Emery-Dreifuss muscular dystrophy 2, a LMNA-linked disease affecting skeletal and cardiac muscles, demonstrated that Ankrd2 is a lamin A-binding protein and that mutated lamins found in Emery-Dreifuss muscular dystrophy change the dynamics of Ankrd2 nuclear import, thus affecting oxidative stress response. In this review, besides describing the latest advances related to Ankrd2 studies, including novel discoveries on Ankrd2 isoform-specific functions, we report the main findings on the relationship of Ankrd2 with A-type lamins and discuss known and potential mechanisms involving defective Ankrd2-lamin A interplay in the pathogenesis of muscular laminopathies.",
publisher = "Hindawi Ltd, London",
journal = "Oxidative Medicine and Cellular Longevity",
title = "Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies",
volume = "2019",
doi = "10.1155/2019/7318796"
}

Cenni, V., Kojić, S., Capanni, C., Faulkner, G.,& Lattanzi, G.. (2019). Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies. in Oxidative Medicine and Cellular Longevity
Hindawi Ltd, London., 2019.
https://doi.org/10.1155/2019/7318796

Cenni V, Kojić S, Capanni C, Faulkner G, Lattanzi G. Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies. in Oxidative Medicine and Cellular Longevity. 2019;2019.
doi:10.1155/2019/7318796 .

Cenni, Vittoria, Kojić, Snežana, Capanni, Cristina, Faulkner, Georgine, Lattanzi, Giovanna, "Ankrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular Laminopathies" in Oxidative Medicine and Cellular Longevity, 2019 (2019),
https://doi.org/10.1155/2019/7318796 . .

TY  - JOUR
AU  - Bošković, Srđan
AU  - Marin-Juez, Ruben
AU  - Jasnić, Jovana
AU  - Reischauer, Sven
AU  - El Sammak, Hadil
AU  - Kojić, Ana
AU  - Faulkner, Georgine
AU  - Radojković, Dragica
AU  - Stainier, Didier Y. R.
AU  - Kojić, Snežana
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1141
AB  - Muscle proteins with ankyrin repeats (MARPs) ANKRD1 and ANKRD2 are titin-associated proteins with a putative role as transcriptional co-regulators in striated muscle, involved in the cellular response to mechanical, oxidative and metabolic stress. Since many aspects of the biology of MARPs, particularly exact mechanisms of their action, in striated muscle are still elusive, research in this field will benefit from novel animal model system. Here we investigated the MARPs found in zebrafish for protein structure, evolutionary conservation, spatiotemporal expression profiles and response to increased muscle activity. Ankrd1 and Ankrd2 show overall moderate conservation at the protein level, more pronounced in the region of ankyrin repeats, motifs indispensable for their function. The two zebrafish genes, ankrd1a and ankrd1b, counterparts of mammalian ANKRD1/Ankrd1, have different expression profiles during first seven days of development. Mild increase of ankrd1a transcript levels was detected at 72 hpf (1.74 +/- 0.24 fold increase relative to 24 hpf time point), while ankrd1b expression was markedly upregulated from 24 hpf onward and peaked at 72 hpf (92.18 +/- 36.95 fold increase relative to 24 hpf time point). Spatially, they exhibited non-overlapping expression patterns during skeletal muscle development in trunk (ankrd1a) and tail (ankrd1b) somites. Expression of ankrd2 was barely detectable. Zebrafish MARPs, expressed at a relatively low level in adult striated muscle, were found to be responsive to endurance exercise training consisting of two bouts of 3 hours of forced swimming daily, for five consecutive days. Three hours after the last exercise bout, ankrd1a expression increased in cardiac muscle (6.19 +/- 5.05 fold change), while ankrd1b and ankrd2 were upregulated in skeletal muscle (1.97 +/- 1.05 and 1.84 +/- 0.58 fold change, respectively). This study provides the foundation to establish zebrafish as a novel in vivo model for further investigation of MARPs function in striated muscle.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise
IS  - 9
VL  - 13
DO  - 10.1371/journal.pone.0204312
ER  - 

@article{
author = "Bošković, Srđan and Marin-Juez, Ruben and Jasnić, Jovana and Reischauer, Sven and El Sammak, Hadil and Kojić, Ana and Faulkner, Georgine and Radojković, Dragica and Stainier, Didier Y. R. and Kojić, Snežana",
year = "2018",
abstract = "Muscle proteins with ankyrin repeats (MARPs) ANKRD1 and ANKRD2 are titin-associated proteins with a putative role as transcriptional co-regulators in striated muscle, involved in the cellular response to mechanical, oxidative and metabolic stress. Since many aspects of the biology of MARPs, particularly exact mechanisms of their action, in striated muscle are still elusive, research in this field will benefit from novel animal model system. Here we investigated the MARPs found in zebrafish for protein structure, evolutionary conservation, spatiotemporal expression profiles and response to increased muscle activity. Ankrd1 and Ankrd2 show overall moderate conservation at the protein level, more pronounced in the region of ankyrin repeats, motifs indispensable for their function. The two zebrafish genes, ankrd1a and ankrd1b, counterparts of mammalian ANKRD1/Ankrd1, have different expression profiles during first seven days of development. Mild increase of ankrd1a transcript levels was detected at 72 hpf (1.74 +/- 0.24 fold increase relative to 24 hpf time point), while ankrd1b expression was markedly upregulated from 24 hpf onward and peaked at 72 hpf (92.18 +/- 36.95 fold increase relative to 24 hpf time point). Spatially, they exhibited non-overlapping expression patterns during skeletal muscle development in trunk (ankrd1a) and tail (ankrd1b) somites. Expression of ankrd2 was barely detectable. Zebrafish MARPs, expressed at a relatively low level in adult striated muscle, were found to be responsive to endurance exercise training consisting of two bouts of 3 hours of forced swimming daily, for five consecutive days. Three hours after the last exercise bout, ankrd1a expression increased in cardiac muscle (6.19 +/- 5.05 fold change), while ankrd1b and ankrd2 were upregulated in skeletal muscle (1.97 +/- 1.05 and 1.84 +/- 0.58 fold change, respectively). This study provides the foundation to establish zebrafish as a novel in vivo model for further investigation of MARPs function in striated muscle.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise",
number = "9",
volume = "13",
doi = "10.1371/journal.pone.0204312"
}

Bošković, S., Marin-Juez, R., Jasnić, J., Reischauer, S., El Sammak, H., Kojić, A., Faulkner, G., Radojković, D., Stainier, D. Y. R.,& Kojić, S.. (2018). Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise. in PLoS One
Public Library Science, San Francisco., 13(9).
https://doi.org/10.1371/journal.pone.0204312

Bošković S, Marin-Juez R, Jasnić J, Reischauer S, El Sammak H, Kojić A, Faulkner G, Radojković D, Stainier DYR, Kojić S. Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise. in PLoS One. 2018;13(9).
doi:10.1371/journal.pone.0204312 .

Bošković, Srđan, Marin-Juez, Ruben, Jasnić, Jovana, Reischauer, Sven, El Sammak, Hadil, Kojić, Ana, Faulkner, Georgine, Radojković, Dragica, Stainier, Didier Y. R., Kojić, Snežana, "Characterization of zebrafish (Danio rerio) muscle ankyrin repeat proteins reveals their conserved response to endurance exercise" in PLoS One, 13, no. 9 (2018),
https://doi.org/10.1371/journal.pone.0204312 . .

TY  - JOUR
AU  - Jasnić, Jovana
AU  - Krause, Sabine
AU  - Savić, Slobodan
AU  - Kojić, Ana
AU  - Kovcić, Vlado
AU  - Bošković, Srđan
AU  - Nestorović, Aleksandra
AU  - Rakićević, Ljiljana
AU  - Schreiber-Katz, Olivia
AU  - Vogel, Johannes G.
AU  - Schoser, Benedikt G.
AU  - Walter, Maggie C.
AU  - Valle, Giorgio
AU  - Radojković, Dragica
AU  - Faulkner, Georgine
AU  - Kojić, Snežana
PY  - 2016
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/933
AB  - Four human Ankrd2 transcripts, reported in the Ensembl database, code for distinct protein isoforms (360, 333, 327 and 300 aa), and so far, their existence, specific expression and localization patterns have not been studied in detail. Ankrd2 is preferentially expressed in the slow fibers of skeletal muscle. It is found in both the nuclei and the cytoplasm of skeletal muscle cells, and its localization is prone to change during differentiation and upon stress. Ankrd2 has also been detected in the heart, in ventricular cardiomyocytes and in the intercalated disks (ICDs). The main objective of this study was to distinguish between the Ankrd2 isoforms and to determine the contribution of each one to the general profile of Ankrd2 expression in striated muscles. We demonstrated that the known expression and localization pattern of Ankrd2 in striated muscle can be attributed to the isoform of 333 aa which is dominant in both tissues, while the designated cardiac and canonical isoform of 360 aa was less expressed in both tissues. The 360 aa isoform has a distinct nuclear localization in human skeletal muscle, as well as in primary myoblasts and myotubes. In contrast to the isoform of 333 aa, it was not preferentially expressed in slow fibers and not localized to the ICDs of human cardiomyocytes. Regulation of the expression of both isoforms is achieved at the transcriptional level. Our results set the stage for investigation of the specific functions and interactions of the Ankrd2 isoforms in healthy and diseased human striated muscles.
PB  - Springer, New York
T2  - Histochemistry and Cell Biology
T1  - Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles
EP  - 584
IS  - 5
SP  - 569
VL  - 146
DO  - 10.1007/s00418-016-1465-0
ER  - 

@article{
author = "Jasnić, Jovana and Krause, Sabine and Savić, Slobodan and Kojić, Ana and Kovcić, Vlado and Bošković, Srđan and Nestorović, Aleksandra and Rakićević, Ljiljana and Schreiber-Katz, Olivia and Vogel, Johannes G. and Schoser, Benedikt G. and Walter, Maggie C. and Valle, Giorgio and Radojković, Dragica and Faulkner, Georgine and Kojić, Snežana",
year = "2016",
abstract = "Four human Ankrd2 transcripts, reported in the Ensembl database, code for distinct protein isoforms (360, 333, 327 and 300 aa), and so far, their existence, specific expression and localization patterns have not been studied in detail. Ankrd2 is preferentially expressed in the slow fibers of skeletal muscle. It is found in both the nuclei and the cytoplasm of skeletal muscle cells, and its localization is prone to change during differentiation and upon stress. Ankrd2 has also been detected in the heart, in ventricular cardiomyocytes and in the intercalated disks (ICDs). The main objective of this study was to distinguish between the Ankrd2 isoforms and to determine the contribution of each one to the general profile of Ankrd2 expression in striated muscles. We demonstrated that the known expression and localization pattern of Ankrd2 in striated muscle can be attributed to the isoform of 333 aa which is dominant in both tissues, while the designated cardiac and canonical isoform of 360 aa was less expressed in both tissues. The 360 aa isoform has a distinct nuclear localization in human skeletal muscle, as well as in primary myoblasts and myotubes. In contrast to the isoform of 333 aa, it was not preferentially expressed in slow fibers and not localized to the ICDs of human cardiomyocytes. Regulation of the expression of both isoforms is achieved at the transcriptional level. Our results set the stage for investigation of the specific functions and interactions of the Ankrd2 isoforms in healthy and diseased human striated muscles.",
publisher = "Springer, New York",
journal = "Histochemistry and Cell Biology",
title = "Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles",
pages = "584-569",
number = "5",
volume = "146",
doi = "10.1007/s00418-016-1465-0"
}

Jasnić, J., Krause, S., Savić, S., Kojić, A., Kovcić, V., Bošković, S., Nestorović, A., Rakićević, L., Schreiber-Katz, O., Vogel, J. G., Schoser, B. G., Walter, M. C., Valle, G., Radojković, D., Faulkner, G.,& Kojić, S.. (2016). Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles. in Histochemistry and Cell Biology
Springer, New York., 146(5), 569-584.
https://doi.org/10.1007/s00418-016-1465-0

Jasnić J, Krause S, Savić S, Kojić A, Kovcić V, Bošković S, Nestorović A, Rakićević L, Schreiber-Katz O, Vogel JG, Schoser BG, Walter MC, Valle G, Radojković D, Faulkner G, Kojić S. Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles. in Histochemistry and Cell Biology. 2016;146(5):569-584.
doi:10.1007/s00418-016-1465-0 .

Jasnić, Jovana, Krause, Sabine, Savić, Slobodan, Kojić, Ana, Kovcić, Vlado, Bošković, Srđan, Nestorović, Aleksandra, Rakićević, Ljiljana, Schreiber-Katz, Olivia, Vogel, Johannes G., Schoser, Benedikt G., Walter, Maggie C., Valle, Giorgio, Radojković, Dragica, Faulkner, Georgine, Kojić, Snežana, "Differential expression and localization of Ankrd2 isoforms in human skeletal and cardiac muscles" in Histochemistry and Cell Biology, 146, no. 5 (2016):569-584,
https://doi.org/10.1007/s00418-016-1465-0 . .

TY  - JOUR
AU  - Jasnić, Jovana
AU  - Nestorović, Aleksandra
AU  - Savić, Slobodan
AU  - Karasek, Sinisa
AU  - Vitulo, Nicola
AU  - Valle, Giorgio
AU  - Faulkner, Georgine
AU  - Radojković, Dragica
AU  - Kojić, Snežana
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/814
AB  - Muscle-specific mechanosensors Ankrd2/Arpp (ankyrin repeat protein 2) and Ankrd1/CARP (cardiac ankyrin repeat protein) have an important role in transcriptional regulation, myofibrillar assembly, cardiogenesis and myogenesis. In skeletal muscle myofibrils, Ankrd2 has a structural role as a component of a titin associated stretch-sensing complex, while in the nucleus it exerts regulatory function as transcriptional co-factor. It is also involved in myogenic differentiation and coordination of myoblast proliferation. Although expressed in the heart, the role of Ankrd2 in the cardiac muscle is completely unknown. Recently, we have shown that hypertrophic and dilated cardiomyopathy pathways are altered upon Ankrd2 silencing suggesting the importance of this protein in cardiac tissue. Here we provide the underlying basis for the functional investigation of Ankrd2 in the heart. We confirmed reduced Ankrd2 expression levels in human heart in comparison with Ankrd1 using RNAseq and Western blot. For the first time we demonstrated that, apart from the sarcomere and nucleus, both proteins are localized to the intercalated disks of human cardiomyocytes. We further tested the expression and localization of endogenous Ankrd2 in rat neonatal cardiomyocytes, a well-established model for studying cardiac-specific proteins. Ankrd2 was found to be expressed in both the cytoplasm and nucleus, independently from maturation status of cardiomyocytes. In contrast to Ankrd1, it is not responsive to the cardiotoxic drug Doxorubicin, suggesting that different mechanisms govern their expression in cardiac cells.
PB  - Springer, New York
T2  - Histochemistry and Cell Biology
T1  - Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes
EP  - 597
IS  - 6
SP  - 583
VL  - 143
DO  - 10.1007/s00418-015-1307-5
ER  - 

@article{
author = "Jasnić, Jovana and Nestorović, Aleksandra and Savić, Slobodan and Karasek, Sinisa and Vitulo, Nicola and Valle, Giorgio and Faulkner, Georgine and Radojković, Dragica and Kojić, Snežana",
year = "2015",
abstract = "Muscle-specific mechanosensors Ankrd2/Arpp (ankyrin repeat protein 2) and Ankrd1/CARP (cardiac ankyrin repeat protein) have an important role in transcriptional regulation, myofibrillar assembly, cardiogenesis and myogenesis. In skeletal muscle myofibrils, Ankrd2 has a structural role as a component of a titin associated stretch-sensing complex, while in the nucleus it exerts regulatory function as transcriptional co-factor. It is also involved in myogenic differentiation and coordination of myoblast proliferation. Although expressed in the heart, the role of Ankrd2 in the cardiac muscle is completely unknown. Recently, we have shown that hypertrophic and dilated cardiomyopathy pathways are altered upon Ankrd2 silencing suggesting the importance of this protein in cardiac tissue. Here we provide the underlying basis for the functional investigation of Ankrd2 in the heart. We confirmed reduced Ankrd2 expression levels in human heart in comparison with Ankrd1 using RNAseq and Western blot. For the first time we demonstrated that, apart from the sarcomere and nucleus, both proteins are localized to the intercalated disks of human cardiomyocytes. We further tested the expression and localization of endogenous Ankrd2 in rat neonatal cardiomyocytes, a well-established model for studying cardiac-specific proteins. Ankrd2 was found to be expressed in both the cytoplasm and nucleus, independently from maturation status of cardiomyocytes. In contrast to Ankrd1, it is not responsive to the cardiotoxic drug Doxorubicin, suggesting that different mechanisms govern their expression in cardiac cells.",
publisher = "Springer, New York",
journal = "Histochemistry and Cell Biology",
title = "Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes",
pages = "597-583",
number = "6",
volume = "143",
doi = "10.1007/s00418-015-1307-5"
}

Jasnić, J., Nestorović, A., Savić, S., Karasek, S., Vitulo, N., Valle, G., Faulkner, G., Radojković, D.,& Kojić, S.. (2015). Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes. in Histochemistry and Cell Biology
Springer, New York., 143(6), 583-597.
https://doi.org/10.1007/s00418-015-1307-5

Jasnić J, Nestorović A, Savić S, Karasek S, Vitulo N, Valle G, Faulkner G, Radojković D, Kojić S. Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes. in Histochemistry and Cell Biology. 2015;143(6):583-597.
doi:10.1007/s00418-015-1307-5 .

Jasnić, Jovana, Nestorović, Aleksandra, Savić, Slobodan, Karasek, Sinisa, Vitulo, Nicola, Valle, Giorgio, Faulkner, Georgine, Radojković, Dragica, Kojić, Snežana, "Profiling of skeletal muscle Ankrd2 protein in human cardiac tissue and neonatal rat cardiomyocytes" in Histochemistry and Cell Biology, 143, no. 6 (2015):583-597,
https://doi.org/10.1007/s00418-015-1307-5 . .

TY  - JOUR
AU  - Kojić, Snežana
AU  - Nestorović, Aleksandra
AU  - Rakićević, Ljiljana
AU  - Protić, Olga
AU  - Jasnić, Jovana
AU  - Faulkner, Georgine
AU  - Radojković, Dragica
PY  - 2015
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/879
AB  - Transcription factor Nkx2.5, essential for heart development, regulates cardiomyocyte-specific gene expression through combinatorial interactions with other cardiac-restricted (GATA4 and dHAND) or ubiquitous (p300) transcription regulators. Here we demonstrate that Nkx2.5 and p53 synergistically activate the promoter of the striated muscle stress responsive transcriptional cofactor Ankrd2, involved in coordination of proliferation and apoptosis during myogenic differentiation. Moreover, the p53 protein is able to interact with both wild type Nkx2.5 and its mutant Delta Nkx2.5 (aa 1-198) found in patients with diverse cardiac malformations. Nkx2.5 interaction site of p53 maps to the C terminal region, while p53 binding site on Nkx2.5 lies outside its C terminus. In addition, overexpression of Nkx2.5 has a modulatory, promoter dependent effect on p53 transactivation, while the mutant significantly abolished p53 activity on the Mdm2, p21(WAF1/CIP1) and Box promoters. Their physical interaction contributes to the observed behavior in the case of the Mdm2 promoter. Our data provide a new evidence for the role of p53 in cardiac function through interaction with Nkx2.5.
PB  - Elsevier Science Inc, New York
T2  - Archives of Biochemistry and Biophysics
T1  - Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity
EP  - 53
SP  - 45
VL  - 569
DO  - 10.1016/j.abb.2015.02.001
ER  - 

@article{
author = "Kojić, Snežana and Nestorović, Aleksandra and Rakićević, Ljiljana and Protić, Olga and Jasnić, Jovana and Faulkner, Georgine and Radojković, Dragica",
year = "2015",
abstract = "Transcription factor Nkx2.5, essential for heart development, regulates cardiomyocyte-specific gene expression through combinatorial interactions with other cardiac-restricted (GATA4 and dHAND) or ubiquitous (p300) transcription regulators. Here we demonstrate that Nkx2.5 and p53 synergistically activate the promoter of the striated muscle stress responsive transcriptional cofactor Ankrd2, involved in coordination of proliferation and apoptosis during myogenic differentiation. Moreover, the p53 protein is able to interact with both wild type Nkx2.5 and its mutant Delta Nkx2.5 (aa 1-198) found in patients with diverse cardiac malformations. Nkx2.5 interaction site of p53 maps to the C terminal region, while p53 binding site on Nkx2.5 lies outside its C terminus. In addition, overexpression of Nkx2.5 has a modulatory, promoter dependent effect on p53 transactivation, while the mutant significantly abolished p53 activity on the Mdm2, p21(WAF1/CIP1) and Box promoters. Their physical interaction contributes to the observed behavior in the case of the Mdm2 promoter. Our data provide a new evidence for the role of p53 in cardiac function through interaction with Nkx2.5.",
publisher = "Elsevier Science Inc, New York",
journal = "Archives of Biochemistry and Biophysics",
title = "Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity",
pages = "53-45",
volume = "569",
doi = "10.1016/j.abb.2015.02.001"
}

Kojić, S., Nestorović, A., Rakićević, L., Protić, O., Jasnić, J., Faulkner, G.,& Radojković, D.. (2015). Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity. in Archives of Biochemistry and Biophysics
Elsevier Science Inc, New York., 569, 45-53.
https://doi.org/10.1016/j.abb.2015.02.001

Kojić S, Nestorović A, Rakićević L, Protić O, Jasnić J, Faulkner G, Radojković D. Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity. in Archives of Biochemistry and Biophysics. 2015;569:45-53.
doi:10.1016/j.abb.2015.02.001 .

Kojić, Snežana, Nestorović, Aleksandra, Rakićević, Ljiljana, Protić, Olga, Jasnić, Jovana, Faulkner, Georgine, Radojković, Dragica, "Cardiac transcription factor Nkx2.5 interacts with p53 and modulates its activity" in Archives of Biochemistry and Biophysics, 569 (2015):45-53,
https://doi.org/10.1016/j.abb.2015.02.001 . .

TY  - JOUR
AU  - Martinelli, Valentina C.
AU  - Kyle, W. Buck
AU  - Kojić, Snežana
AU  - Vitulo, Nicola
AU  - Li, Zhaohui
AU  - Belgrano, Anna
AU  - Maiuri, Paolo
AU  - Banks, Lawrence
AU  - Vatta, Matteo
AU  - Valle, Giorgio
AU  - Faulkner, Georgine
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/780
AB  - ZASP is a cytoskeletal PDZ-LIM protein predominantly expressed in striated muscle. It forms multiprotein complexes and plays a pivotal role in the structural integrity of sarcomeres. Mutations in the ZASP protein are associated with myofibrillar myopathy, left ventricular non-compaction and dilated cardiomyopathy. The ablation of its murine homologue Cypher results in neonatal lethality. ZASP has several alternatively spliced isoforms, in this paper we clarify the nomenclature of its human isoforms as well as their dynamics and expression pattern in striated muscle. Interaction is demonstrated between ZASP and two new binding partners both of which have roles in signalling, regulation of gene expression and muscle differentiation; the mechanosensing protein Ankrd2 and the tumour suppressor protein p53. These proteins and ZASP form a triple complex that appears to facilitate poly-SUMOylation of p53. We also show the importance of two of its functional domains, the ZM-motif and the PDZ domain. The PDZ domain can bind directly to both Ankrd2 and p53 indicating that there is no competition between it and p53 for the same binding site on Ankrd2. However there is competition for this binding site between p53 and a region of the ZASP protein lacking the PDZ domain, but containing the ZM-motif. ZASP is negative regulator of p53 in transactivation experiments with the p53-responsive promoters, MDM2 and BAX. Mutations in the ZASP ZM-motif induce modification in protein turnover. In fact, two mutants, A165V and A171T, were not able to bind Ankrd2 and bound only poorly to alpha-actinin2. This is important since the A165V mutation is responsible for zaspopathy, a well characterized autosomal dominant distal myopathy. Although the mechanism by which this mutant causes disease is still unknown, this is the first indication of how a ZASP disease associated mutant protein differs from that of the wild type ZASP protein.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - ZASP Interacts with the Mechanosensing Protein Ankrd2 and p53 in the Signalling Network of Striated Muscle
IS  - 3
VL  - 9
DO  - 10.1371/journal.pone.0092259
ER  - 

@article{
author = "Martinelli, Valentina C. and Kyle, W. Buck and Kojić, Snežana and Vitulo, Nicola and Li, Zhaohui and Belgrano, Anna and Maiuri, Paolo and Banks, Lawrence and Vatta, Matteo and Valle, Giorgio and Faulkner, Georgine",
year = "2014",
abstract = "ZASP is a cytoskeletal PDZ-LIM protein predominantly expressed in striated muscle. It forms multiprotein complexes and plays a pivotal role in the structural integrity of sarcomeres. Mutations in the ZASP protein are associated with myofibrillar myopathy, left ventricular non-compaction and dilated cardiomyopathy. The ablation of its murine homologue Cypher results in neonatal lethality. ZASP has several alternatively spliced isoforms, in this paper we clarify the nomenclature of its human isoforms as well as their dynamics and expression pattern in striated muscle. Interaction is demonstrated between ZASP and two new binding partners both of which have roles in signalling, regulation of gene expression and muscle differentiation; the mechanosensing protein Ankrd2 and the tumour suppressor protein p53. These proteins and ZASP form a triple complex that appears to facilitate poly-SUMOylation of p53. We also show the importance of two of its functional domains, the ZM-motif and the PDZ domain. The PDZ domain can bind directly to both Ankrd2 and p53 indicating that there is no competition between it and p53 for the same binding site on Ankrd2. However there is competition for this binding site between p53 and a region of the ZASP protein lacking the PDZ domain, but containing the ZM-motif. ZASP is negative regulator of p53 in transactivation experiments with the p53-responsive promoters, MDM2 and BAX. Mutations in the ZASP ZM-motif induce modification in protein turnover. In fact, two mutants, A165V and A171T, were not able to bind Ankrd2 and bound only poorly to alpha-actinin2. This is important since the A165V mutation is responsible for zaspopathy, a well characterized autosomal dominant distal myopathy. Although the mechanism by which this mutant causes disease is still unknown, this is the first indication of how a ZASP disease associated mutant protein differs from that of the wild type ZASP protein.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "ZASP Interacts with the Mechanosensing Protein Ankrd2 and p53 in the Signalling Network of Striated Muscle",
number = "3",
volume = "9",
doi = "10.1371/journal.pone.0092259"
}

Martinelli, V. C., Kyle, W. B., Kojić, S., Vitulo, N., Li, Z., Belgrano, A., Maiuri, P., Banks, L., Vatta, M., Valle, G.,& Faulkner, G.. (2014). ZASP Interacts with the Mechanosensing Protein Ankrd2 and p53 in the Signalling Network of Striated Muscle. in PLoS One
Public Library Science, San Francisco., 9(3).
https://doi.org/10.1371/journal.pone.0092259

Martinelli VC, Kyle WB, Kojić S, Vitulo N, Li Z, Belgrano A, Maiuri P, Banks L, Vatta M, Valle G, Faulkner G. ZASP Interacts with the Mechanosensing Protein Ankrd2 and p53 in the Signalling Network of Striated Muscle. in PLoS One. 2014;9(3).
doi:10.1371/journal.pone.0092259 .

Martinelli, Valentina C., Kyle, W. Buck, Kojić, Snežana, Vitulo, Nicola, Li, Zhaohui, Belgrano, Anna, Maiuri, Paolo, Banks, Lawrence, Vatta, Matteo, Valle, Giorgio, Faulkner, Georgine, "ZASP Interacts with the Mechanosensing Protein Ankrd2 and p53 in the Signalling Network of Striated Muscle" in PLoS One, 9, no. 3 (2014),
https://doi.org/10.1371/journal.pone.0092259 . .

TY  - JOUR
AU  - Nestorović, Aleksandra
AU  - Jasnić, Jovana
AU  - Faulkner, Georgine
AU  - Radojković, Dragica
AU  - Kojić, Snežana
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/736
AB  - The muscle ankyrin repeat protein Ankrd1 is localized in a mechanosensory complex of the sarcomeric I-band. It is involved in signaling pathways activated in response to mechanical stretch. It also acts as a transcriptional cofactor in the nucleus, playing an important role in cardiogenesis and skeletal muscle differentiation. To investigate its regulatory function in signaling we employed protein array methodology and identified 10 novel Ankrd1 binding partners among PDZ domain proteins known to act as platforms for multiprotein complex assembly. The zonula occludens protein-1 (ZO-1) was chosen for further analysis since its interaction with Ankrd2 had already been demonstrated. Both Ankrd2 and Ankrd1 have similar functions and localize in the same regions. We confirmed the interaction of Ankrd1 with ZO-1 protein and determined their subcellular distribution in HeLa cells, showing their colocalization in the cytoplasm. Our findings corroborate the role of Ankrd1 in intracellular signaling.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1
EP  - 1242
IS  - 3
SP  - 1233
VL  - 66
DO  - 10.2298/ABS1403233N
ER  - 

@article{
author = "Nestorović, Aleksandra and Jasnić, Jovana and Faulkner, Georgine and Radojković, Dragica and Kojić, Snežana",
year = "2014",
abstract = "The muscle ankyrin repeat protein Ankrd1 is localized in a mechanosensory complex of the sarcomeric I-band. It is involved in signaling pathways activated in response to mechanical stretch. It also acts as a transcriptional cofactor in the nucleus, playing an important role in cardiogenesis and skeletal muscle differentiation. To investigate its regulatory function in signaling we employed protein array methodology and identified 10 novel Ankrd1 binding partners among PDZ domain proteins known to act as platforms for multiprotein complex assembly. The zonula occludens protein-1 (ZO-1) was chosen for further analysis since its interaction with Ankrd2 had already been demonstrated. Both Ankrd2 and Ankrd1 have similar functions and localize in the same regions. We confirmed the interaction of Ankrd1 with ZO-1 protein and determined their subcellular distribution in HeLa cells, showing their colocalization in the cytoplasm. Our findings corroborate the role of Ankrd1 in intracellular signaling.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1",
pages = "1242-1233",
number = "3",
volume = "66",
doi = "10.2298/ABS1403233N"
}

Nestorović, A., Jasnić, J., Faulkner, G., Radojković, D.,& Kojić, S.. (2014). Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 66(3), 1233-1242.
https://doi.org/10.2298/ABS1403233N

Nestorović A, Jasnić J, Faulkner G, Radojković D, Kojić S. Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1. in Archives of Biological Sciences. 2014;66(3):1233-1242.
doi:10.2298/ABS1403233N .

Nestorović, Aleksandra, Jasnić, Jovana, Faulkner, Georgine, Radojković, Dragica, Kojić, Snežana, "Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1" in Archives of Biological Sciences, 66, no. 3 (2014):1233-1242,
https://doi.org/10.2298/ABS1403233N . .

TY  - JOUR
AU  - Kojić, Snežana
AU  - Radojković, Dragica
AU  - Faulkner, Georgine
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/493
AB  - Remodeling is a stringently controlled process that enables adequate response of muscle cells to constant physical stresses. In this process, different kinds of stimuli have to be sensed and converted into biochemical signals that ultimately lead to alterations of muscle phenotype. Several multiprotein complexes located in the sarcomere and organized on the titin molecular spring have been identified as stress sensors and signal transducers. In this review, we focus on Ankrd1/CARP and Ankrd2/Arpp proteins, which belong to the muscle ankyrin repeat protein family (MARP) involved in a mechano-signaling pathway that links myofibrillar stress response to muscle gene expression. Apart from the mechanosensory function, they have an important role in transcriptional regulation, myofibrillar assembly, cardiogenesis and myogenesis. Their altered expression has been demonstrated in neuromuscular disorders, cardiovascular diseases, as well as in tumors, suggesting a role in pathological processes. Although analyzed in a limited number of patients, there is a considerable body of evidence that MARP proteins could be suitable candidates for prognostic and diagnostic biomarkers.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Critical Reviews in Clinical Laboratory Sciences
T1  - Muscle ankyrin repeat proteins: their role in striated muscle function in health and disease
EP  - 294
IS  - 5-6
SP  - 269
VL  - 48
DO  - 10.3109/10408363.2011.643857
ER  - 

@article{
author = "Kojić, Snežana and Radojković, Dragica and Faulkner, Georgine",
year = "2011",
abstract = "Remodeling is a stringently controlled process that enables adequate response of muscle cells to constant physical stresses. In this process, different kinds of stimuli have to be sensed and converted into biochemical signals that ultimately lead to alterations of muscle phenotype. Several multiprotein complexes located in the sarcomere and organized on the titin molecular spring have been identified as stress sensors and signal transducers. In this review, we focus on Ankrd1/CARP and Ankrd2/Arpp proteins, which belong to the muscle ankyrin repeat protein family (MARP) involved in a mechano-signaling pathway that links myofibrillar stress response to muscle gene expression. Apart from the mechanosensory function, they have an important role in transcriptional regulation, myofibrillar assembly, cardiogenesis and myogenesis. Their altered expression has been demonstrated in neuromuscular disorders, cardiovascular diseases, as well as in tumors, suggesting a role in pathological processes. Although analyzed in a limited number of patients, there is a considerable body of evidence that MARP proteins could be suitable candidates for prognostic and diagnostic biomarkers.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Critical Reviews in Clinical Laboratory Sciences",
title = "Muscle ankyrin repeat proteins: their role in striated muscle function in health and disease",
pages = "294-269",
number = "5-6",
volume = "48",
doi = "10.3109/10408363.2011.643857"
}

Kojić, S., Radojković, D.,& Faulkner, G.. (2011). Muscle ankyrin repeat proteins: their role in striated muscle function in health and disease. in Critical Reviews in Clinical Laboratory Sciences
Taylor & Francis Ltd, Abingdon., 48(5-6), 269-294.
https://doi.org/10.3109/10408363.2011.643857

Kojić S, Radojković D, Faulkner G. Muscle ankyrin repeat proteins: their role in striated muscle function in health and disease. in Critical Reviews in Clinical Laboratory Sciences. 2011;48(5-6):269-294.
doi:10.3109/10408363.2011.643857 .

Kojić, Snežana, Radojković, Dragica, Faulkner, Georgine, "Muscle ankyrin repeat proteins: their role in striated muscle function in health and disease" in Critical Reviews in Clinical Laboratory Sciences, 48, no. 5-6 (2011):269-294,
https://doi.org/10.3109/10408363.2011.643857 . .

TY  - JOUR
AU  - Belgrano, Anna
AU  - Rakićević, Ljiljana
AU  - Mittempergher, Lorenza
AU  - Campanaro, Stefano
AU  - Martinelli, Valentina C.
AU  - Mouly, Vincent
AU  - Valle, Giorgio
AU  - Kojić, Snežana
AU  - Faulkner, Georgine
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/502
AB  - Background: Ankrd2 (also known as Arpp) together with Ankrd1/CARP and DARP are members of the MARP mechanosensing proteins that form a complex with titin (N2A)/calpain 3 protease/myopalladin. In muscle, Ankrd2 is located in the I-band of the sarcomere and moves to the nucleus of adjacent myofibers on muscle injury. In myoblasts it is predominantly in the nucleus and on differentiation shifts from the nucleus to the cytoplasm. In agreement with its role as a sensor it interacts both with sarcomeric proteins and transcription factors. Methodology/Principal Findings: Expression profiling of endogenous Ankrd2 silenced in human myotubes was undertaken to elucidate its role as an intermediary in cell signaling pathways. Silencing Ankrd2 expression altered the expression of genes involved in both intercellular communication (cytokine-cytokine receptor interaction, endocytosis, focal adhesion, tight junction, gap junction and regulation of the actin cytoskeleton) and intracellular communication (calcium, insulin, MAPK, p53, TGF-beta and Wnt signaling). The significance of Ankrd2 in cell signaling was strengthened by the fact that we were able to show for the first time that Nkx2.5 and p53 are upstream effectors of the Ankrd2 gene and that Ankrd1/CARP, another MARP member, can modulate the transcriptional ability of MyoD on the Ankrd2 promoter. Another novel finding was the interaction between Ankrd2 and proteins with PDZ and SH3 domains, further supporting its role in signaling. It is noteworthy that we demonstrated that transcription factors PAX6, LHX2, NFIL3 and MECP2, were able to bind both the Ankrd2 protein and its promoter indicating the presence of a regulatory feedback loop mechanism. Conclusions/Significance: In conclusion we demonstrate that Ankrd2 is a potent regulator in muscle cells affecting a multitude of pathways and processes.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Multi-Tasking Role of the Mechanosensing Protein Ankrd2 in the Signaling Network of Striated Muscle
IS  - 10
VL  - 6
DO  - 10.1371/journal.pone.0025519
ER  - 

@article{
author = "Belgrano, Anna and Rakićević, Ljiljana and Mittempergher, Lorenza and Campanaro, Stefano and Martinelli, Valentina C. and Mouly, Vincent and Valle, Giorgio and Kojić, Snežana and Faulkner, Georgine",
year = "2011",
abstract = "Background: Ankrd2 (also known as Arpp) together with Ankrd1/CARP and DARP are members of the MARP mechanosensing proteins that form a complex with titin (N2A)/calpain 3 protease/myopalladin. In muscle, Ankrd2 is located in the I-band of the sarcomere and moves to the nucleus of adjacent myofibers on muscle injury. In myoblasts it is predominantly in the nucleus and on differentiation shifts from the nucleus to the cytoplasm. In agreement with its role as a sensor it interacts both with sarcomeric proteins and transcription factors. Methodology/Principal Findings: Expression profiling of endogenous Ankrd2 silenced in human myotubes was undertaken to elucidate its role as an intermediary in cell signaling pathways. Silencing Ankrd2 expression altered the expression of genes involved in both intercellular communication (cytokine-cytokine receptor interaction, endocytosis, focal adhesion, tight junction, gap junction and regulation of the actin cytoskeleton) and intracellular communication (calcium, insulin, MAPK, p53, TGF-beta and Wnt signaling). The significance of Ankrd2 in cell signaling was strengthened by the fact that we were able to show for the first time that Nkx2.5 and p53 are upstream effectors of the Ankrd2 gene and that Ankrd1/CARP, another MARP member, can modulate the transcriptional ability of MyoD on the Ankrd2 promoter. Another novel finding was the interaction between Ankrd2 and proteins with PDZ and SH3 domains, further supporting its role in signaling. It is noteworthy that we demonstrated that transcription factors PAX6, LHX2, NFIL3 and MECP2, were able to bind both the Ankrd2 protein and its promoter indicating the presence of a regulatory feedback loop mechanism. Conclusions/Significance: In conclusion we demonstrate that Ankrd2 is a potent regulator in muscle cells affecting a multitude of pathways and processes.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Multi-Tasking Role of the Mechanosensing Protein Ankrd2 in the Signaling Network of Striated Muscle",
number = "10",
volume = "6",
doi = "10.1371/journal.pone.0025519"
}

Belgrano, A., Rakićević, L., Mittempergher, L., Campanaro, S., Martinelli, V. C., Mouly, V., Valle, G., Kojić, S.,& Faulkner, G.. (2011). Multi-Tasking Role of the Mechanosensing Protein Ankrd2 in the Signaling Network of Striated Muscle. in PLoS One
Public Library Science, San Francisco., 6(10).
https://doi.org/10.1371/journal.pone.0025519

Belgrano A, Rakićević L, Mittempergher L, Campanaro S, Martinelli VC, Mouly V, Valle G, Kojić S, Faulkner G. Multi-Tasking Role of the Mechanosensing Protein Ankrd2 in the Signaling Network of Striated Muscle. in PLoS One. 2011;6(10).
doi:10.1371/journal.pone.0025519 .

Belgrano, Anna, Rakićević, Ljiljana, Mittempergher, Lorenza, Campanaro, Stefano, Martinelli, Valentina C., Mouly, Vincent, Valle, Giorgio, Kojić, Snežana, Faulkner, Georgine, "Multi-Tasking Role of the Mechanosensing Protein Ankrd2 in the Signaling Network of Striated Muscle" in PLoS One, 6, no. 10 (2011),
https://doi.org/10.1371/journal.pone.0025519 . .

TY  - JOUR
AU  - Kojić, Snežana
AU  - Nestorović, Aleksandra
AU  - Rakićević, Ljiljana
AU  - Belgrano, Anna
AU  - Stanković, Marija
AU  - Divac Rankov, Aleksandra
AU  - Faulkner, Georgine
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/445
AB  - The muscle ankyrin repeat protein (MARP) family member Ankrd1/CARP is a part of the titin-mechanosensory signaling complex in the sarcomere and in response to stretch it translocates to the nucleus where it participates in the regulation of cardiac genes as a transcriptional co-repressor. Several studies have focused on its structural role in muscle, but its regulatory role is still poorly understood To gain more insight into the regulatory function of Ankrd1/CARP we searched for transcription factors that could interact and modulate its activity. Using protein array methodology we identified the tumor suppressor protein p53 as an Ankrd1/CARP interacting partner and confirmed their interaction both in vivo and in vitro We demonstrate a novel role for Ankrd1/CARP as a transcriptional co-activator, moderately up regulating p53 activity Furthermore, we show that p53 operates as an upstream effector of Ankrd1/CARP, by up regulating the proximal ANKRD1 promoter Our findings suggest that, besides acting as a transcriptional co-repressor, Ankrd1/CARP could have a stimulatory effect on gene expression in cultured skeletal muscle cells It is probable that Ankrd1 /CARP has a role in the propagation of signals initiated by myogenic regulatory factors (MRFs) during myogenesis
PB  - Elsevier Science Inc, New York
T2  - Archives of Biochemistry and Biophysics
T1  - A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein
EP  - 67
IS  - 1
SP  - 60
VL  - 502
DO  - 10.1016/j.abb.2010.06.029
ER  - 

@article{
author = "Kojić, Snežana and Nestorović, Aleksandra and Rakićević, Ljiljana and Belgrano, Anna and Stanković, Marija and Divac Rankov, Aleksandra and Faulkner, Georgine",
year = "2010",
abstract = "The muscle ankyrin repeat protein (MARP) family member Ankrd1/CARP is a part of the titin-mechanosensory signaling complex in the sarcomere and in response to stretch it translocates to the nucleus where it participates in the regulation of cardiac genes as a transcriptional co-repressor. Several studies have focused on its structural role in muscle, but its regulatory role is still poorly understood To gain more insight into the regulatory function of Ankrd1/CARP we searched for transcription factors that could interact and modulate its activity. Using protein array methodology we identified the tumor suppressor protein p53 as an Ankrd1/CARP interacting partner and confirmed their interaction both in vivo and in vitro We demonstrate a novel role for Ankrd1/CARP as a transcriptional co-activator, moderately up regulating p53 activity Furthermore, we show that p53 operates as an upstream effector of Ankrd1/CARP, by up regulating the proximal ANKRD1 promoter Our findings suggest that, besides acting as a transcriptional co-repressor, Ankrd1/CARP could have a stimulatory effect on gene expression in cultured skeletal muscle cells It is probable that Ankrd1 /CARP has a role in the propagation of signals initiated by myogenic regulatory factors (MRFs) during myogenesis",
publisher = "Elsevier Science Inc, New York",
journal = "Archives of Biochemistry and Biophysics",
title = "A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein",
pages = "67-60",
number = "1",
volume = "502",
doi = "10.1016/j.abb.2010.06.029"
}

Kojić, S., Nestorović, A., Rakićević, L., Belgrano, A., Stanković, M., Divac Rankov, A.,& Faulkner, G.. (2010). A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein. in Archives of Biochemistry and Biophysics
Elsevier Science Inc, New York., 502(1), 60-67.
https://doi.org/10.1016/j.abb.2010.06.029

Kojić S, Nestorović A, Rakićević L, Belgrano A, Stanković M, Divac Rankov A, Faulkner G. A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein. in Archives of Biochemistry and Biophysics. 2010;502(1):60-67.
doi:10.1016/j.abb.2010.06.029 .

Kojić, Snežana, Nestorović, Aleksandra, Rakićević, Ljiljana, Belgrano, Anna, Stanković, Marija, Divac Rankov, Aleksandra, Faulkner, Georgine, "A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein" in Archives of Biochemistry and Biophysics, 502, no. 1 (2010):60-67,
https://doi.org/10.1016/j.abb.2010.06.029 . .

TY  - JOUR
AU  - Kojić, Snežana
AU  - Medeot, Elisa
AU  - Faulkner, Georgine
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/384
AB  - Protein Ankrd2 poseduje ankirinske ponovke, specifično se eksprimira u skeletnim mišićima i srcu i može biti lokalizovan i u jedru i u citoplazmi mišićne ćelije Pošto antitela na ovaj protein nisu komercijalno dostupna, u ovom radu je opisano generisanje i karakterizacija tri mišja poliklonska i jednog monoklonskog antitela dobijenih na ceo, kao i na amino-terminalni i karboksi-terminalni deo proteina. Korišćenjem rekombinantnih deletanata mapiran je epitop monoklonskog antitela veličine 10 aminokiselina (323-333 ak), a takođe je pokazano da poliklonska antitela na amino-terminalni i karboksiterminalni deo proteina specifično prepoznaju Ankrd2, a ne ankirinske ponovke koji su prisutni u velikom broju­proteina. Sva četiri antitela su visoko specifična za endogeni Ankrd2 koji se eksprimira u srcu i skeletnim mišićima.
AB  - In order to study the function of the Ankrd2 protein, for which commercial antibodies are not available, we report the production and analysis of polyclonal antibodies to full-length Ankrd2 and its C-terminal and N-terminal regions, as well as a monoclonal antibody to the C-terminus of the protein. Epitope mapping making use of recombinant deletion mutants showed that an epitope located in region 323-333 aa of Ankrd2 is detected by the monoclonal antibody. The high specificity of all four anti-Ankrd2 antibodies for recombinant and endogenous Ankrd2 protein is also demon­strated.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Karakterizacija antitela na humani mišićni protein Ankrd2
T1  - Characterization of antibodies directed against the Ankrd2 human muscle protein
EP  - 691
IS  - 4
SP  - 683
VL  - 61
DO  - 10.2298/ABS0904683K
ER  - 

@article{
author = "Kojić, Snežana and Medeot, Elisa and Faulkner, Georgine",
year = "2009",
abstract = "Protein Ankrd2 poseduje ankirinske ponovke, specifično se eksprimira u skeletnim mišićima i srcu i može biti lokalizovan i u jedru i u citoplazmi mišićne ćelije Pošto antitela na ovaj protein nisu komercijalno dostupna, u ovom radu je opisano generisanje i karakterizacija tri mišja poliklonska i jednog monoklonskog antitela dobijenih na ceo, kao i na amino-terminalni i karboksi-terminalni deo proteina. Korišćenjem rekombinantnih deletanata mapiran je epitop monoklonskog antitela veličine 10 aminokiselina (323-333 ak), a takođe je pokazano da poliklonska antitela na amino-terminalni i karboksiterminalni deo proteina specifično prepoznaju Ankrd2, a ne ankirinske ponovke koji su prisutni u velikom broju­proteina. Sva četiri antitela su visoko specifična za endogeni Ankrd2 koji se eksprimira u srcu i skeletnim mišićima., In order to study the function of the Ankrd2 protein, for which commercial antibodies are not available, we report the production and analysis of polyclonal antibodies to full-length Ankrd2 and its C-terminal and N-terminal regions, as well as a monoclonal antibody to the C-terminus of the protein. Epitope mapping making use of recombinant deletion mutants showed that an epitope located in region 323-333 aa of Ankrd2 is detected by the monoclonal antibody. The high specificity of all four anti-Ankrd2 antibodies for recombinant and endogenous Ankrd2 protein is also demon­strated.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Karakterizacija antitela na humani mišićni protein Ankrd2, Characterization of antibodies directed against the Ankrd2 human muscle protein",
pages = "691-683",
number = "4",
volume = "61",
doi = "10.2298/ABS0904683K"
}

Kojić, S., Medeot, E.,& Faulkner, G.. (2009). Karakterizacija antitela na humani mišićni protein Ankrd2. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 61(4), 683-691.
https://doi.org/10.2298/ABS0904683K

Kojić S, Medeot E, Faulkner G. Karakterizacija antitela na humani mišićni protein Ankrd2. in Archives of Biological Sciences. 2009;61(4):683-691.
doi:10.2298/ABS0904683K .

Kojić, Snežana, Medeot, Elisa, Faulkner, Georgine, "Karakterizacija antitela na humani mišićni protein Ankrd2" in Archives of Biological Sciences, 61, no. 4 (2009):683-691,
https://doi.org/10.2298/ABS0904683K . .

TY  - JOUR
AU  - Pallavicini, Alberto
AU  - Kojić, Snežana
AU  - Bean, Camilla
AU  - Vainzof, Mariz
AU  - Salamon, Michela
AU  - Ievolella, Chiara
AU  - Bortoletto, Gladis
AU  - Pacchioni, Beniamima
AU  - Zatz, Mayana
AU  - Lanfranchi, Gerolamo
AU  - Faulkner, Georgine
AU  - Valle, Giorgio
PY  - 2001
UR  - https://www.sciencedirect.com/science/article/pii/S0006291X01951319
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2301
AB  - Human Ankrd2 transcript encodes a 37-kDa protein that is similar to mouse Ankrd2 recently shown to be involved in hypertrophy of skeletal muscle. These novel ankyrin-rich proteins are related to C-193/CARP/MARP, a cardiac protein involved in the control of cardiac hypertrophy. A human genomic region of 14,300 bp was sequenced revealing a gene organization similar to mouse Ankrd2 with nine exons, four of which encode ankyrin repeats. The intracellular localization of Ankrd2 was unknown since no protein studies had been reported. In this paper we studied the intracellular localization of the protein and its expression on differentiation using polyclonal and monoclonal antibodies produced to human Ankrd2. In adult skeletal muscle Ankrd2 is found in slow fibers; however, not all of the slow fibers express Ankrd2 at the same level. This is particularly evident in dystrophic muscles, where the expression of Ankrd2 in slow fibers seems to be severely reduced.
PB  - Elsevier
T2  - Biochemical and Biophysical Research Communications
T2  - Biochemical and Biophysical Research CommunicationsBiochemical and Biophysical Research Communications
T1  - Characterization of Human Skeletal Muscle Ankrd2
EP  - 386
IS  - 2
SP  - 378
VL  - 285
DO  - 10.1006/bbrc.2001.5131
ER  - 

@article{
author = "Pallavicini, Alberto and Kojić, Snežana and Bean, Camilla and Vainzof, Mariz and Salamon, Michela and Ievolella, Chiara and Bortoletto, Gladis and Pacchioni, Beniamima and Zatz, Mayana and Lanfranchi, Gerolamo and Faulkner, Georgine and Valle, Giorgio",
year = "2001",
abstract = "Human Ankrd2 transcript encodes a 37-kDa protein that is similar to mouse Ankrd2 recently shown to be involved in hypertrophy of skeletal muscle. These novel ankyrin-rich proteins are related to C-193/CARP/MARP, a cardiac protein involved in the control of cardiac hypertrophy. A human genomic region of 14,300 bp was sequenced revealing a gene organization similar to mouse Ankrd2 with nine exons, four of which encode ankyrin repeats. The intracellular localization of Ankrd2 was unknown since no protein studies had been reported. In this paper we studied the intracellular localization of the protein and its expression on differentiation using polyclonal and monoclonal antibodies produced to human Ankrd2. In adult skeletal muscle Ankrd2 is found in slow fibers; however, not all of the slow fibers express Ankrd2 at the same level. This is particularly evident in dystrophic muscles, where the expression of Ankrd2 in slow fibers seems to be severely reduced.",
publisher = "Elsevier",
journal = "Biochemical and Biophysical Research Communications, Biochemical and Biophysical Research CommunicationsBiochemical and Biophysical Research Communications",
title = "Characterization of Human Skeletal Muscle Ankrd2",
pages = "386-378",
number = "2",
volume = "285",
doi = "10.1006/bbrc.2001.5131"
}

Pallavicini, A., Kojić, S., Bean, C., Vainzof, M., Salamon, M., Ievolella, C., Bortoletto, G., Pacchioni, B., Zatz, M., Lanfranchi, G., Faulkner, G.,& Valle, G.. (2001). Characterization of Human Skeletal Muscle Ankrd2. in Biochemical and Biophysical Research Communications
Elsevier., 285(2), 378-386.
https://doi.org/10.1006/bbrc.2001.5131

Pallavicini A, Kojić S, Bean C, Vainzof M, Salamon M, Ievolella C, Bortoletto G, Pacchioni B, Zatz M, Lanfranchi G, Faulkner G, Valle G. Characterization of Human Skeletal Muscle Ankrd2. in Biochemical and Biophysical Research Communications. 2001;285(2):378-386.
doi:10.1006/bbrc.2001.5131 .

Pallavicini, Alberto, Kojić, Snežana, Bean, Camilla, Vainzof, Mariz, Salamon, Michela, Ievolella, Chiara, Bortoletto, Gladis, Pacchioni, Beniamima, Zatz, Mayana, Lanfranchi, Gerolamo, Faulkner, Georgine, Valle, Giorgio, "Characterization of Human Skeletal Muscle Ankrd2" in Biochemical and Biophysical Research Communications, 285, no. 2 (2001):378-386,
https://doi.org/10.1006/bbrc.2001.5131 . .