Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1
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 cardiogene...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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University of Belgrade, University of Novi Sad
2014-01-01
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| Series: | Archives of Biological Sciences |
| Subjects: | |
| Online Access: | http://www.doiserbia.nb.rs/img/doi/0354-4664/2014/0354-46641403233N.pdf |
| _version_ | 1819067724153749504 |
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| author | Nestorović Aleksandra Jasnic-Savovic Jovana Faulkner Georgine Radojković Dragica Kojić Snežana |
| author_facet | Nestorović Aleksandra Jasnic-Savovic Jovana Faulkner Georgine Radojković Dragica Kojić Snežana |
| author_sort | Nestorović Aleksandra |
| collection | DOAJ |
| description | 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. [Projekat
Ministarstva nauke Republike Srbije, br. ON173008] |
| first_indexed | 2024-12-21T16:22:48Z |
| format | Article |
| id | doaj.art-c1eb7ace2de24707855fdd4fe06b3af7 |
| institution | Directory Open Access Journal |
| issn | 0354-4664 1821-4339 |
| language | English |
| last_indexed | 2024-12-21T16:22:48Z |
| publishDate | 2014-01-01 |
| publisher | University of Belgrade, University of Novi Sad |
| record_format | Article |
| series | Archives of Biological Sciences |
| spelling | doaj.art-c1eb7ace2de24707855fdd4fe06b3af72022-12-21T18:57:31ZengUniversity of Belgrade, University of Novi SadArchives of Biological Sciences0354-46641821-43392014-01-016631233124210.2298/ABS1403233N0354-46641403233NAnkrd1-mediated signaling is supported by its interaction with zonula occludens-1Nestorović Aleksandra0Jasnic-Savovic Jovana1Faulkner Georgine2Radojković Dragica3Kojić Snežana4Institute of Molecular Genetics and Genetic Engineering, BelgradeInstitute of Molecular Genetics and Genetic Engineering, BelgradeCRIBI, University of Padua, Padua, ItalyInstitute of Molecular Genetics and Genetic Engineering, BelgradeInstitute of Molecular Genetics and Genetic Engineering, BelgradeThe 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. [Projekat Ministarstva nauke Republike Srbije, br. ON173008]http://www.doiserbia.nb.rs/img/doi/0354-4664/2014/0354-46641403233N.pdfmuscle ankyrin repeat proteinsPDZprotein arrayprotein-protein interactionsignaling |
| spellingShingle | Nestorović Aleksandra Jasnic-Savovic Jovana Faulkner Georgine Radojković Dragica Kojić Snežana Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1 Archives of Biological Sciences muscle ankyrin repeat proteins PDZ protein array protein-protein interaction signaling |
| title | Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1 |
| title_full | Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1 |
| title_fullStr | Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1 |
| title_full_unstemmed | Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1 |
| title_short | Ankrd1-mediated signaling is supported by its interaction with zonula occludens-1 |
| title_sort | ankrd1 mediated signaling is supported by its interaction with zonula occludens 1 |
| topic | muscle ankyrin repeat proteins PDZ protein array protein-protein interaction signaling |
| url | http://www.doiserbia.nb.rs/img/doi/0354-4664/2014/0354-46641403233N.pdf |
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