Journal Article

PreJuSER-14490

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Tyrosine phosphorylation of vinculin at position 1065 modifies focal adhesion dynamics and cell tractions

Küpper, K.FZJ* ; Lang, N.FZJ* ; Möhl, C.FZJ* ; Kirchgeßner, N.FZJ* ; Born, S.FZJ* ; Goldmann, W. H.FZJ* ; Hoffmann, B.FZJ* ; Merkel, R.FZJ*

2010
Academic Press Orlando, Fla.

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Please use a persistent id in citations: doi:10.1016/j.bbrc.2010.07.110

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.

Keyword(s): Animals (MeSH) ; Focal Adhesions: genetics (MeSH) ; Focal Adhesions: metabolism (MeSH) ; Mice (MeSH) ; Mice, Knockout (MeSH) ; Mutation (MeSH) ; Phosphorylation (MeSH) ; Tyrosine: genetics (MeSH) ; Tyrosine: metabolism (MeSH) ; Vinculin: genetics (MeSH) ; Vinculin: metabolism (MeSH) ; Vinculin ; Tyrosine ; J ; Vinculin (auto) ; Focal adhesion dynamics (auto) ; Fluorescence recovery after photobleaching (auto) ; Cell tractions (auto) ; Tyrosine phosphorylation (auto)

Note: 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).

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Contributing Institute(s):

1. Biomechanik (IBN-4)

Research Program(s):

1. BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung (P45)

Appears in the scientific report 2010

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