Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion

Abstract

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.

DOI: 10.1083/jcb.201112129

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@inproceedings{Zhang2012ArginylationdependentRO, title={Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion}, author={Fangliang Zhang and Sougata Saha and Anna Kashina}, booktitle={The Journal of cell biology}, year={2012} }