This title appears in the Scientific Report :
2009
Please use the identifier:
http://dx.doi.org/10.1002/cm.20375 in citations.
Becoming Stable and Strong: The Interplay between Vinculin Exchange Dynamics and Adhesion Strength During Adhesion Site Maturation
Becoming Stable and Strong: The Interplay between Vinculin Exchange Dynamics and Adhesion Strength During Adhesion Site Maturation
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....
Saved in:
Personal Name(s): | Möhl, C. |
---|---|
Kirchgeßner, N. / Schäfer, C. / Küpper, K. / Born, S. / Diez, G. / Goldmann, W.H. / Merkel, R. / Hoffmann, B. | |
Contributing Institute: |
Biomechanik; IBN-4 |
Published in: | Cell Motility and the Cytoskeleton, 66 (2009) S. 350 - 364 |
Imprint: |
Bognor Regis
Wiley
2009
|
Physical Description: |
350 - 364 |
DOI: |
10.1002/cm.20375 |
PubMed ID: |
19422016 |
Document Type: |
Journal Article |
Research Program: |
Kondensierte Materie |
Series Title: |
Cell Motility and the Cytoskeleton
66 |
Subject (ZB): | |
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245 | |a Becoming Stable and Strong: The Interplay between Vinculin Exchange Dynamics and Adhesion Strength During Adhesion Site Maturation | ||
260 | |c 2009 |a Bognor Regis |b Wiley | ||
300 | |a 350 - 364 | ||
440 | 0 | |a Cell Motility and the Cytoskeleton |x 0886-1544 |0 20941 |y 6 |v 66 | |
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520 | |a 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. | ||
588 | |a Dataset connected to Web of Science, Pubmed | ||
650 | 2 | |2 MeSH |a Cell Adhesion: physiology | |
650 | 2 | |2 MeSH |a Cell Movement: physiology | |
650 | 2 | |2 MeSH |a Cells, Cultured | |
650 | 2 | |2 MeSH |a Fluorescence Recovery After Photobleaching | |
650 | 2 | |2 MeSH |a Focal Adhesions: metabolism | |
650 | 2 | |2 MeSH |a Humans | |
650 | 2 | |2 MeSH |a Keratinocytes: cytology | |
650 | 2 | |2 MeSH |a Keratinocytes: metabolism | |
650 | 2 | |2 MeSH |a Phosphorylation: physiology | |
650 | 2 | |2 MeSH |a Vinculin: genetics | |
650 | 2 | |2 MeSH |a Vinculin: metabolism | |
650 | 7 | |0 125361-02-6 |2 NLM Chemicals |a Vinculin | |
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653 | 2 | 0 | |2 Author |a vinculin |
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653 | 2 | 0 | |2 Author |a exchange dynamics |
653 | 2 | 0 | |2 Author |a focal adhesion |
653 | 2 | 0 | |2 Author |a cell force |
653 | 2 | 0 | |2 Author |a tyrosine phosphorylation |
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