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Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion
Talin is a large scaffolding molecule that plays a major role in integrin-dependent cell–matrix adhesion. A role for talin in cell–cell attachment through cadherin has never been demonstrated, however. Here, we identify a novel calpain-dependent proteolytic cleavage of talin that results in the rele...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3373405/ https://www.ncbi.nlm.nih.gov/pubmed/22665520 http://dx.doi.org/10.1083/jcb.201112129 |
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author | Zhang, Fangliang Saha, Sougata Kashina, Anna |
author_facet | Zhang, Fangliang Saha, Sougata Kashina, Anna |
author_sort | Zhang, Fangliang |
collection | PubMed |
description | Talin is a large scaffolding molecule that plays a major role in integrin-dependent cell–matrix adhesion. A role for talin in cell–cell attachment through cadherin has never been demonstrated, however. Here, we identify a novel calpain-dependent proteolytic cleavage of talin that results in the release of a 70-kD C-terminal fragment, which serves as a substrate of posttranslational arginylation. The intracellular levels of this fragment closely correlated with the formation of cell–cell adhesions, and this fragment localized to cadherin-containing cell–cell contacts. Moreover, reintroduction of this fragment rescued the cell–cell adhesion defects in arginyltransferase (Ate1) knockout cells, which normally have a very low level of this fragment. Arginylation of this fragment further enhanced its ability to rescue cell–cell adhesion formation. In addition, arginylation facilitated its turnover, suggesting a dual role of arginylation in its intracellular regulation. Thus, our work identifies a novel proteolytic product of talin that is regulated by arginylation and a new role of talin in cadherin-dependent cell–cell adhesion. |
format | Online Article Text |
id | pubmed-3373405 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-33734052012-12-11 Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion Zhang, Fangliang Saha, Sougata Kashina, Anna J Cell Biol Research Articles Talin is a large scaffolding molecule that plays a major role in integrin-dependent cell–matrix adhesion. A role for talin in cell–cell attachment through cadherin has never been demonstrated, however. Here, we identify a novel calpain-dependent proteolytic cleavage of talin that results in the release of a 70-kD C-terminal fragment, which serves as a substrate of posttranslational arginylation. The intracellular levels of this fragment closely correlated with the formation of cell–cell adhesions, and this fragment localized to cadherin-containing cell–cell contacts. Moreover, reintroduction of this fragment rescued the cell–cell adhesion defects in arginyltransferase (Ate1) knockout cells, which normally have a very low level of this fragment. Arginylation of this fragment further enhanced its ability to rescue cell–cell adhesion formation. In addition, arginylation facilitated its turnover, suggesting a dual role of arginylation in its intracellular regulation. Thus, our work identifies a novel proteolytic product of talin that is regulated by arginylation and a new role of talin in cadherin-dependent cell–cell adhesion. The Rockefeller University Press 2012-06-11 /pmc/articles/PMC3373405/ /pubmed/22665520 http://dx.doi.org/10.1083/jcb.201112129 Text en © 2012 Zhang et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Zhang, Fangliang Saha, Sougata Kashina, Anna Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion |
title | Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion |
title_full | Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion |
title_fullStr | Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion |
title_full_unstemmed | Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion |
title_short | Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion |
title_sort | arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3373405/ https://www.ncbi.nlm.nih.gov/pubmed/22665520 http://dx.doi.org/10.1083/jcb.201112129 |
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