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  Molecular complexity and dynamics of cell-matrix adhesions

Zamir, E., & Geiger, B. (2001). Molecular complexity and dynamics of cell-matrix adhesions. Journal of Cell Science, 114(Pt 20), 3583-3590. Retrieved from http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11707510.

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Genre: Zeitschriftenartikel
Alternativer Titel : J Cell Sci

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 Urheber:
Zamir, E.1, Autor           
Geiger, B., Autor
Affiliations:
1Abt. II: Systemische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753288              

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Schlagwörter: Cell Adhesion/*physiology; Cell-Matrix Junctions/*physiology; Cytoskeleton/metabolism; Extracellular Matrix/metabolism; Fibroblasts/cytology/metabolism; Humans; Integrins/metabolism; Intercellular Junctions/chemistry/metabolism; Microfilament Proteins/metabolism; Microscopy, Fluorescence; Models, Biological; Vinculin/metabolism
 Zusammenfassung: Currently >50 proteins have been reported to be associated with focal contacts and related ECM adhesions. Most of these contain multiple domains through which they can interact with different molecular partners, potentially forming a dense and heterogeneous protein network at the cytoplasmic faces of the adhesion site. The molecular and structural diversity of this 'submembrane plaque' is regulated by a wide variety of mechanisms, including competition between different partner proteins for the same binding sites, interactions triggered or suppressed by tyrosine phosphorylation, and conformational changes in component proteins, which can affect their reactivity. Indeed, integrin-mediated adhesions can undergo dynamic changes in structure and molecular properties from dot-like focal complexes to stress-fiber-associated focal contacts, which can further 'mature' to form fibronectin-bound fibrillar adhesions. These changes are driven by mechanical force generated by the actin- and myosin-containing contractile machinery of the cells, or by external forces applied to the cells, and regulated by matrix rigidity.

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 Datum: 2001-10
 Publikationsstatus: Erschienen
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Titel: Journal of Cell Science
  Alternativer Titel : J Cell Sci
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 114 (Pt 20) Artikelnummer: - Start- / Endseite: 3583 - 3590 Identifikator: ISSN: 0021-9533 (Print)