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  Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner

Carisey, A., Tsang, R., Greiner, A. M., Nijenhuis, N., Heath, N., Nazgiewicz, A., et al. (2013). Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner. Current Biology, 23(4), 271-281. doi:10.1016/j.cub.2013.01.009.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-E3C7-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-767C-A
Genre: Journal Article

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CurrBiol_23_2013_271.pdf (Any fulltext), 3MB
 
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 Creators:
Carisey, Alex, Author
Tsang, Ricky, Author
Greiner, Alexandra M., Author
Nijenhuis, Nadja, Author
Heath, Nikki, Author
Nazgiewicz, Alicja, Author
Kemkemer, Ralf1, Author              
Derby, Brian, Author
Spatz, Joachim P.1, 2, Author              
Ballestrem, Christoph, Author
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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Free keywords: Abt. Spatz, ZWE Biomaterialien
 Abstract: BACKGROUND: Cells sense the extracellular environment using adhesion receptors (integrins) linked to the intracellular actin cytoskeleton through a complex network of regulatory proteins that, all together, form focal adhesions (FAs). The molecular basis of how these sensing units are regulated, how they are implicated in transducing mechanical stimuli, and how this leads to a spatiotemporal coordination of FAs is unclear. RESULTS: Here we show that vinculin, through its links to the talin-integrin complex and F-actin, regulates the transmission of mechanical signals from the extracellular matrix to the actomyosin machinery. We demonstrate that the vinculin interaction with the talin-integrin complex drives the recruitment and release of core FA components. The activation state of vinculin is itself regulated by force, as underscored by our observation that vinculin localization to FAs is dependent on actomyosin contraction. Using a variety of vinculin mutants, we establish which components of the cell-matrix adhesion network are coordinated through direct and indirect associations with vinculin. Moreover, using cyclic stretching, we demonstrate that vinculin plays a key role in the transmission of extracellular mechanical stimuli leading to the reorganization of cell polarity. Of particular importance is the actin-binding tail region of vinculin, without which the cell's ability to repolarize in response to cyclic stretching is perturbed. CONCLUSIONS: Overall our data promote a model whereby vinculin controls the transmission of intracellular and extracellular mechanical cues that are important for the spatiotemporal assembly, disassembly, and reorganization of FAs to coordinate polarized cell motility.

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Language(s): eng - English
 Dates: 2013-11-162013-07-292013-01-022013-01-312013-02-18
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Current Biology
  Other : Curr. Biol.
Source Genre: Journal
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Publ. Info: London, UK : Cell Press
Pages: - Volume / Issue: 23 (4) Sequence Number: - Start / End Page: 271 - 281 Identifier: ISSN: 0960-9822
CoNE: https://pure.mpg.de/cone/journals/resource/954925579107