1986
DOI: 10.1038/320531a0
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Interaction of plasma membrane fibronectin receptor with talin—a transmembrane linkage

Abstract: Many observations suggest the presence of transmembrane linkages between the cytoskeleton and the extracellular matrix. In fibroblasts both light and electron microscopic observations reveal a co-alignment between actin filaments at the cell surface and extracellular fibronectin. These associations are seen at sites of cell matrix interaction, frequently along stress fibres and sometimes where these bundles of microfilaments terminate at adhesion plaques (focal contacts). Non-morphological evidence also indica… Show more

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Cited by 1,149 publications
(574 citation statements)
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References 28 publications
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“…These molecules make up the VLA proteins (33). p, is widely distributed in human cells and tissues (34) and may be involved in transmembrane signal transduction via interaction with cytoskeletal elements (35). In our study, p,-integrin (CD29) was present to a greater extent on most cell types in noninflammatory tissues.…”
Section: Discussionmentioning
confidence: 45%
“…These molecules make up the VLA proteins (33). p, is widely distributed in human cells and tissues (34) and may be involved in transmembrane signal transduction via interaction with cytoskeletal elements (35). In our study, p,-integrin (CD29) was present to a greater extent on most cell types in noninflammatory tissues.…”
Section: Discussionmentioning
confidence: 45%
“…For example, both talin and paxillin are unique in that they are known to bind to the focal adhesion targeting sequence of FAK (Schaller, 1996) and talin also binds directly to the integrin cytoplasmic β tail (Horwitz et al, 1986). Paxillin is also a substrate for FAK and src kinase activity and hence a potential signal initiator (Subauste et al, 2004).…”
Section: Integrins and Integrin Associated Proteinsmentioning
confidence: 99%
“…This is thought to be achieved in part by calpain cleavage of talin, a cytoskeletal anchor that links integrins to actin filaments. Calpain cleavage of talin exposes the N-terminal FERM domain that is then free to bind directly to integrin β subunits [187][188][189] and forge linkages with actin filaments.…”
Section: Regulation Of Focal Adhesions and Actin By Proteolysismentioning
confidence: 99%