| First Author | Bays JL | Year | 2014 |
| Journal | J Cell Biol | Volume | 205 |
| Issue | 2 | Pages | 251-63 |
| PubMed ID | 24751539 | Mgi Jnum | J:215836 |
| Mgi Id | MGI:5607189 | Doi | 10.1083/jcb.201309092 |
| Citation | Bays JL, et al. (2014) Vinculin phosphorylation differentially regulates mechanotransduction at cell-cell and cell-matrix adhesions. J Cell Biol 205(2):251-63 |
| abstractText | Cells experience mechanical forces throughout their lifetimes. Vinculin is critical for transmitting these forces, yet how it achieves its distinct functions at cell-cell and cell-matrix adhesions remains unanswered. Here, we show vinculin is phosphorylated at Y822 in cell-cell, but not cell-matrix, adhesions. Phosphorylation at Y822 was elevated when forces were applied to E-cadherin and was required for vinculin to integrate into the cadherin complex. The mutation Y822F ablated these activities and prevented cells from stiffening in response to forces on E-cadherin. In contrast, Y822 phosphorylation was not required for vinculin functions in cell-matrix adhesions, including integrin-induced cell stiffening. Finally, forces applied to E-cadherin activated Abelson (Abl) tyrosine kinase to phosphorylate vinculin; Abl inhibition mimicked the loss of vinculin phosphorylation. These data reveal an unexpected regulatory mechanism in which vinculin Y822 phosphorylation determines whether cadherins transmit force and provides a paradigm for how a shared component of adhesions can produce biologically distinct functions. |
