Journal Article

PreJuSER-4910

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Becoming Stable and Strong: The Interplay between Vinculin Exchange Dynamics and Adhesion Strength During Adhesion Site Maturation

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

2009
Wiley Bognor Regis

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Please use a persistent id in citations: doi:10.1002/cm.20375

Abstract: The coordinated formation and release of focal adhesions is necessary for cell attachment and migration. According to current models, these processes are caused by temporal variations in protein composition. Protein incorporation into focal adhesions is believed to be controlled by phosphorylation. Here, we tested the exchange dynamics of GFP-vinculin as marker protein of focal adhesions using the method of Fluorescence Recovery After Photobleaching. The relevance of the phosphorylation state of the protein, the age of focal adhesions and the acting force were investigated. For stable focal adhesions of stationary keratinocytes, we determined an exchangeable vinculin fraction of 52% and a recovery halftime of 57 s. Nascent focal adhesions of moving cells contained a fraction of exchanging vinculin of 70% with a recovery halftime of 36 s. Upon maturation, mean saturation values and recovery halftimes decreased to levels of 49% and 42 s, respectively. Additionally, the fraction of stably incorporated vinculin increased with cell forces and decreased with vinculin phosphorylation within these sites. Experiments on a nonphosphorylatable vinculin mutant construct at phosphorylation site tyr1065 confirmed the direct interplay between phosphorylation and exchange dynamics of adhesion proteins during adhesion site maturation.

Keyword(s): Cell Adhesion: physiology (MeSH) ; Cell Movement: physiology (MeSH) ; Cells, Cultured (MeSH) ; Fluorescence Recovery After Photobleaching (MeSH) ; Focal Adhesions: metabolism (MeSH) ; Humans (MeSH) ; Keratinocytes: cytology (MeSH) ; Keratinocytes: metabolism (MeSH) ; Phosphorylation: physiology (MeSH) ; Vinculin: genetics (MeSH) ; Vinculin: metabolism (MeSH) ; Vinculin ; J ; vinculin (auto) ; FRAP (auto) ; exchange dynamics (auto) ; focal adhesion (auto) ; cell force (auto) ; tyrosine phosphorylation (auto)

Note: Contract grant sponsors: BFHZ, BaCaTec, and DAAD.

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Contributing Institute(s):

1. Biomechanik (IBN-4)

Research Program(s):

1. Kondensierte Materie (P54)

Appears in the scientific report 2009

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Database coverage:
; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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