TY  - JOUR
AU  - Küpper, K.
AU  - Lang, N.
AU  - Möhl, C.
AU  - Kirchgeßner, N.
AU  - Born, S.
AU  - Goldmann, W.H.
AU  - Hoffmann, B.
AU  - Merkel, R.
TI  - Tyrosine phosphorylation of vinculin at position 1065 modifies focal adhesion dynamics and cell tractions
JO  - Biochemical and biophysical research communications
VL  - 399
SN  - 0006-291X
CY  - Orlando, Fla.
PB  - Academic Press
M1  - PreJuSER-14490
SP  - 560 - 564
PY  - 2010
N1  - We thank Dr. E.D. Adamson for providing the MEF cells and Dr. B. Fabry for stimulating discussions. We are also indebted to the entire team of IBN 4 for their interlectual input. This work was supported by grants from Bayerisch-Franzosisches Hochschulzentrum, Deutscher Akademischer Austausch Dienst, Bavaria California Technology Center, Deutsche Forschungsgemeinschaft (G0598/13-1), and Bundesministerium fur Bildung und Forschung (Program 0315501).
AB  - 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.
KW  - Animals
KW  - Focal Adhesions: genetics
KW  - Focal Adhesions: metabolism
KW  - Mice
KW  - Mice, Knockout
KW  - Mutation
KW  - Phosphorylation
KW  - Tyrosine: genetics
KW  - Tyrosine: metabolism
KW  - Vinculin: genetics
KW  - Vinculin: metabolism
KW  - Vinculin (NLM Chemicals)
KW  - Tyrosine (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:20678470
UR  - <Go to ISI:>//WOS:000281840200017
DO  - DOI:10.1016/j.bbrc.2010.07.110
UR  - https://juser.fz-juelich.de/record/14490
ER  -