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Tyrosine phosphorylation of vinculin at position 1065 modifies focal adhesion dynamics and cell tractions.

Abstract：

:Focal adhesions (FAs) connect the cellular actin cytoskeleton via integrin with the extracellular matrix. They comprise of many structural and signaling proteins which are highly dynamic, well regulated, and responsible for the sensing of physical properties from the environment. Vinculin is a protein that incorporates all these functions. Here, we investigated the phosphorylation of Y1065 in the activation/regulation of vinculin. We used different vinculin mutants mimicking either a permanently activated or inhibited phosphorylation site at position 1065. Using these mutants, we determined their influence on the exchange dynamics and cell forces using fluorescence recovery after photobleaching and traction microscopy. The results indicate that phosphorylation at Y1065 significantly increases the amount of freely exchanging vinculin within FAs whereas inhibition of this phosphorylation site leads to an uncontrolled exchange of vinculin and reduced adhesive cell forces. In conclusion, we show that phosphorylation on position Y1065 is essential for accurate incorporation of vinculin into FAs and mechanical behavior of cells.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Küpper K,Lang N,Möhl C,Kirchgessner N,Born S,Goldmann WH,Merkel R,Hoffmann B

doi

10.1016/j.bbrc.2010.07.110

subject

Has Abstract

pub_date

2010-09-03 00:00:00

pages

560-4

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(10)01430-0

journal_volume

399

pub_type

杂志文章

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