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Vinculin controls focal adhesion formation by direct interactions with talin and actin.

Vinculin controls focal adhesion formation by direct interactions with talin and actin. Research Abstract Details 

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  • Vinculin controls focal adhesion formation by direct interactions with talin and actin. Abstract Text:

    jonathan d humphriesJonathan D Humphries,pengbo wangPengbo Wang,charles streuliCharles Streuli,benny geigerBenny Geiger,martin j humphriesMartin J Humphries,christoph ballestremChristoph Ballestrem,jonathan d humphriesJonathan D Humphries,pengbo wangPengbo Wang,charles streuliCharles Streuli,benny geigerBenny Geiger,martin j humphriesMartin J Humphries,christoph ballestremChristoph Ballestrem,

    Focal adhesions (FAs) regulate cell migration. Vinculin, with its many potential binding partners, can interconnect signals in FAs. Despite the well-characterized structure of vinculin, the molecular mechanisms underlying its action have remained unclear. Here, using vinculin mutants, we separate the vinculin head and tail regions into distinct functional domains. We show that the vinculin head regulates integrin dynamics and clustering and the tail regulates the link to the mechanotransduction force machinery. The expression of vinculin constructs with unmasked binding sites in the head and tail regions induces dramatic FA growth, which is mediated by their direct interaction with talin. This interaction leads to clustering of activated integrin and an increase in integrin residency time in FAs. Surprisingly, paxillin recruitment, induced by active vinculin constructs, occurs independently of its potential binding site in the vinculin tail. The vinculin tail, however, is responsible for the functional link of FAs to the actin cytoskeleton. We propose a new model that explains how vinculin orchestrates FAs.

    Vinculin controls focal adhesion formation by direct interactions with talin and actin. Publishing Authors By Initials

    jd humphriesJD Humphries,p wangP Wang,c streuliC Streuli,b geigerB Geiger,mj humphriesMJ Humphries,c ballestremC Ballestrem,jd humphriesJD Humphries,p wangP Wang,c streuliC Streuli,b geigerB Geiger,mj humphriesMJ Humphries,c ballestremC Ballestrem,

    For similar proteins: cytoskeletal proteins: vinculin research abstracts see: proteins: cytoskeletal proteins: vinculin research

    PUBMED ID PMID:

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    Vinculin controls focal adhesion formation by direct interactions with talin and actin. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: The Journal of cell biology

    VOLUME: 179

    Page Numbers: 1043-57

    Journal Abbreviation: J. Cell Biol.

    ISSN: 1540-8140

    DAY: 3

    MONTH: Dec

    YEAR: 2007

    Vinculin controls focal adhesion formation by direct interactions with talin and actin. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 375356

    Vinculin controls focal adhesion formation by direct interactions with talin and actin. Keywords Mesh Terms:

    KEYWORDS: Vinculin

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Vinculin controls focal adhesion formation by direct interactions with talin and actin. Information

    Substance Name: Actomyosin

    Registry Number: 9013-26-7

    Grant and Affiliation Information for Vinculin controls focal adhesion formation by direct interactions with talin and actin.

    AFFILIATION: Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester M13 9PT, England, UK.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United Kingdom Wellcome T

    GRANT: 077100

    ACRONYM:

    MEDLINETA: J Cell Biol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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