Talin has a key role in integrin-dependent adhesion of cells to the extracellular matrix, and Kashina and colleagues now report that talin also mediates cell–cell adhesion. A 70 kDa carboxy-terminal fragment (termed VAD) of talin was seen in several cell types and localized at cadherin-containing cell–cell adhesion sites. This fragment was generated through cleavage of talin by the protease calpain 2, and cleavage was dependent on arginylation of VAD. Importantly, arginylation-deficient mutant cells that lacked the VAD fragment formed fewer and smaller cell–cell adhesions, indicating a role for VAD in cell–cell contacts. Furthermore, arginylation was integral in the regulation of VAD function, as arginylated VAD was more efficient in forming cell–cell contacts than its non-arginylated counterpart. Thus, this work uncovers a new role of talin in cadherin-dependent cell–cell adhesion and highlights arginylation as an important post-translational modification.
ORIGINAL RESEARCH PAPER
Zhang, F. et al. Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion. J. Cell Biol. 4 Jun 2012 (doi:10.1083/jcb.201112129)
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Baumann, K. Cell–cell contacts with talin. Nat Rev Mol Cell Biol 13, 409 (2012). https://doi.org/10.1038/nrm3386
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DOI: https://doi.org/10.1038/nrm3386