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  - 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  - 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  - Medeot, E
AU  - Guccione, E
AU  - Krmac, H
AU  - Zara, I
AU  - Martinelli, V
AU  - Valle, G
AU  - Faulkner, G
PY  - 2004
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/195
AB  - Ankrd2 may be a link between the sarcomere and the nucleus; a similar role has recently been proposed for CARP that has a high level of structural and functional conservation with Ankrd2. Both Ankrd2 and CARP are involved in striated muscle hypertrophy. The mechanism by which muscle stretch is sensed and signals are transduced is still unknown; however, Ankrd2 and CARP could play similar roles in pathways leading to hypertrophy, the triggering mechanisms being heart pressure overload monitored by CARP and mechanical stretch in skeletal muscle monitored by Ankrd2. Recently Ankrd2 and CARP have been proposed as members of a family of muscle ankyrin repeat proteins (MARPs) that form a complex with titin, myopalladin and calpain protease p94, involved in signaling and regulation of gene expression in response to muscle stress. Here, we show that Ankrd2 is able to interact with the Z-disc protein telethonin as well as being able to interact with three transcription factors: YB-1, PML and p53. Ankrd2 binding to the ubiquitous transcription factor YB-1 can be demonstrated both in vitro and in vivo; this is not very surprising, since a similar interaction was previously described for CARP. However, the interactions with PML and p53 are unexpected new findings, with interesting implications in the Ankrd2 signaling cascade. Ankrd2 co-localizes with the transcriptional co-activator and co-repressor PML in nuclear bodies (NBs) in human myoblasts as detected by confocal immunofluorescence. Interestingly, we show that Ankrd2 not only binds the tumor suppressor protein p53 both in vitro and in vivo but also enhances the up-regulation of the p21(WAFI/CIPI) promoter by p53. Therefore, our findings strengthen the hypothesis that Ankrd2 may be involved in sensing stress signals and linking these to muscle gene regulation.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Molecular Biology
T1  - The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle
EP  - 325
IS  - 2
SP  - 313
VL  - 339
DO  - 10.1016/j.jmb.2004.03.071
ER  - 

@article{
author = "Kojić, Snežana and Medeot, E and Guccione, E and Krmac, H and Zara, I and Martinelli, V and Valle, G and Faulkner, G",
year = "2004",
abstract = "Ankrd2 may be a link between the sarcomere and the nucleus; a similar role has recently been proposed for CARP that has a high level of structural and functional conservation with Ankrd2. Both Ankrd2 and CARP are involved in striated muscle hypertrophy. The mechanism by which muscle stretch is sensed and signals are transduced is still unknown; however, Ankrd2 and CARP could play similar roles in pathways leading to hypertrophy, the triggering mechanisms being heart pressure overload monitored by CARP and mechanical stretch in skeletal muscle monitored by Ankrd2. Recently Ankrd2 and CARP have been proposed as members of a family of muscle ankyrin repeat proteins (MARPs) that form a complex with titin, myopalladin and calpain protease p94, involved in signaling and regulation of gene expression in response to muscle stress. Here, we show that Ankrd2 is able to interact with the Z-disc protein telethonin as well as being able to interact with three transcription factors: YB-1, PML and p53. Ankrd2 binding to the ubiquitous transcription factor YB-1 can be demonstrated both in vitro and in vivo; this is not very surprising, since a similar interaction was previously described for CARP. However, the interactions with PML and p53 are unexpected new findings, with interesting implications in the Ankrd2 signaling cascade. Ankrd2 co-localizes with the transcriptional co-activator and co-repressor PML in nuclear bodies (NBs) in human myoblasts as detected by confocal immunofluorescence. Interestingly, we show that Ankrd2 not only binds the tumor suppressor protein p53 both in vitro and in vivo but also enhances the up-regulation of the p21(WAFI/CIPI) promoter by p53. Therefore, our findings strengthen the hypothesis that Ankrd2 may be involved in sensing stress signals and linking these to muscle gene regulation.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Molecular Biology",
title = "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle",
pages = "325-313",
number = "2",
volume = "339",
doi = "10.1016/j.jmb.2004.03.071"
}

Kojić, S., Medeot, E., Guccione, E., Krmac, H., Zara, I., Martinelli, V., Valle, G.,& Faulkner, G.. (2004). The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle. in Journal of Molecular Biology
Academic Press Ltd- Elsevier Science Ltd, London., 339(2), 313-325.
https://doi.org/10.1016/j.jmb.2004.03.071

Kojić S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, Valle G, Faulkner G. The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle. in Journal of Molecular Biology. 2004;339(2):313-325.
doi:10.1016/j.jmb.2004.03.071 .

Kojić, Snežana, Medeot, E, Guccione, E, Krmac, H, Zara, I, Martinelli, V, Valle, G, Faulkner, G, "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle" in Journal of Molecular Biology, 339, no. 2 (2004):313-325,
https://doi.org/10.1016/j.jmb.2004.03.071 . .

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 . .

TY  - JOUR
AU  - Pallavicini, A
AU  - Kojić, Snežana
AU  - Bean, C
AU  - Vainzof, M
AU  - Salamon, M
AU  - Ievolella, C
AU  - Bortoletto, G
AU  - Pacchioni, B
AU  - Zatz, M
AU  - Lanfranchi, G
AU  - Faulkner, G
AU  - Valle, G
PY  - 2001
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/148
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  - Academic Press Inc Elsevier Science, San Diego
T2  - Biochemical 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, A and Kojić, Snežana and Bean, C and Vainzof, M and Salamon, M and Ievolella, C and Bortoletto, G and Pacchioni, B and Zatz, M and Lanfranchi, G and Faulkner, G and Valle, G",
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 = "Academic Press Inc Elsevier Science, San Diego",
journal = "Biochemical 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
Academic Press Inc Elsevier Science, San Diego., 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, A, Kojić, Snežana, 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, 285, no. 2 (2001):378-386,
https://doi.org/10.1006/bbrc.2001.5131 . .

TY  - JOUR
AU  - Faulkner, G
AU  - Pallavicini, A
AU  - Comelli, A
AU  - Salamon, M
AU  - Bortoletto, G
AU  - Ievolella, C
AU  - Trevisan, S
AU  - Kojić, Snežana
AU  - Dalla Vecchia, F
AU  - Laveder, P
AU  - Valle, G
AU  - Lanfranchi, G
PY  - 2000
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/142
AB  - We report the identification and characterization of a novel 32-kDa protein expressed in skeletal muscle and located in the Z-disc of the sarcomere. We found that this protein binds to three other Z-disc proteins; therefore, we have-named it FATZ, gamma -filamin/ABP-L, alpha -actinin and telethonin binding protein of the Z-disc. From yeast two-hybrid experiments we are able to show that the SR3-SR4 domains of alpha -actinin 2 are required to bind the COOH-terminal region of the FATZ as does gamma -filamin/ABP-L, Furthermore, by using a glutathione S-transferase overlay assay we find that FATZ also binds telethonin. The level of FATZ protein in muscle cells increases during differentiation, being clearly detectable before the onset of myosin, Although FATZ has no known interaction domains, it would appear to be involved in a complex network of interactions with other Z-band components. On the basis of the information known about its binding partners, we could envisage a central role for FATZ in the: myofibrillogenesis, After screening our muscle expressed sequence tag data base and the public expressed sequence tag data bases, we were able to assemble two other muscle transcripts that show a high level of identity with FATZ in two different domains. Therefore, FATZ may be the first member of a small family of novel muscle proteins.
PB  - Amer Soc Biochemistry Molecular Biology Inc, Rockville
T2  - Journal of Biological Chemistry
T1  - FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle
EP  - 41242
IS  - 52
SP  - 41234
VL  - 275
DO  - 10.1074/jbc.M007493200
ER  - 

@article{
author = "Faulkner, G and Pallavicini, A and Comelli, A and Salamon, M and Bortoletto, G and Ievolella, C and Trevisan, S and Kojić, Snežana and Dalla Vecchia, F and Laveder, P and Valle, G and Lanfranchi, G",
year = "2000",
abstract = "We report the identification and characterization of a novel 32-kDa protein expressed in skeletal muscle and located in the Z-disc of the sarcomere. We found that this protein binds to three other Z-disc proteins; therefore, we have-named it FATZ, gamma -filamin/ABP-L, alpha -actinin and telethonin binding protein of the Z-disc. From yeast two-hybrid experiments we are able to show that the SR3-SR4 domains of alpha -actinin 2 are required to bind the COOH-terminal region of the FATZ as does gamma -filamin/ABP-L, Furthermore, by using a glutathione S-transferase overlay assay we find that FATZ also binds telethonin. The level of FATZ protein in muscle cells increases during differentiation, being clearly detectable before the onset of myosin, Although FATZ has no known interaction domains, it would appear to be involved in a complex network of interactions with other Z-band components. On the basis of the information known about its binding partners, we could envisage a central role for FATZ in the: myofibrillogenesis, After screening our muscle expressed sequence tag data base and the public expressed sequence tag data bases, we were able to assemble two other muscle transcripts that show a high level of identity with FATZ in two different domains. Therefore, FATZ may be the first member of a small family of novel muscle proteins.",
publisher = "Amer Soc Biochemistry Molecular Biology Inc, Rockville",
journal = "Journal of Biological Chemistry",
title = "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle",
pages = "41242-41234",
number = "52",
volume = "275",
doi = "10.1074/jbc.M007493200"
}

Faulkner, G., Pallavicini, A., Comelli, A., Salamon, M., Bortoletto, G., Ievolella, C., Trevisan, S., Kojić, S., Dalla Vecchia, F., Laveder, P., Valle, G.,& Lanfranchi, G.. (2000). FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. in Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc, Rockville., 275(52), 41234-41242.
https://doi.org/10.1074/jbc.M007493200

Faulkner G, Pallavicini A, Comelli A, Salamon M, Bortoletto G, Ievolella C, Trevisan S, Kojić S, Dalla Vecchia F, Laveder P, Valle G, Lanfranchi G. FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. in Journal of Biological Chemistry. 2000;275(52):41234-41242.
doi:10.1074/jbc.M007493200 .

Faulkner, G, Pallavicini, A, Comelli, A, Salamon, M, Bortoletto, G, Ievolella, C, Trevisan, S, Kojić, Snežana, Dalla Vecchia, F, Laveder, P, Valle, G, Lanfranchi, G, "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle" in Journal of Biological Chemistry, 275, no. 52 (2000):41234-41242,
https://doi.org/10.1074/jbc.M007493200 . .