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 . .