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• W2108674983 startingPage "951" @default.
• W2108674983 abstract "We describe a 120-kDa protein (pp120) that is phosphorylated on tyrosine in cells attached to fibronectin-coated surfaces. The protein appears to be located in focal contacts where it codistributes with beta 1 integrins. pp120 is distinct from the beta 1 subunit of integrins and from vinculin and alpha-actinin. pp120 is rapidly dephosphorylated in cells suspended by trypsinization but becomes rapidly phosphorylated in cells attaching and spreading on fibronectin. Attachment of cells to RGD-containing peptides, polylysine, or concanavalin A is not sufficient to induce phosphorylation of pp120. The 120-kDa cell-binding domain of fibronectin can induce some phosphorylation of pp120, but further phosphorylation occurs in the presence also of the heparin-binding domain of fibronectin. Phosphorylation of pp120 precedes, but is correlated with, subsequent cell spreading. Phosphorylation of pp120 can also be triggered by attachment of cells to anti-integrin antibodies, and this requires the cytoplasmic domain of the integrin beta 1 subunit. Thus interaction of beta 1 integrins with extracellular ligands (fibronectin or antibodies) triggers phosphorylation of an intracellular 120-kDa protein, pp120, that may be involved in the responses of cells to attachment." @default.
• W2108674983 created "2016-06-24" @default.
• W2108674983 creator A5030647867 @default.
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• W2108674983 date "1991-11-01" @default.
• W2108674983 modified "2023-10-04" @default.
• W2108674983 title "Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein." @default.
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• W2108674983 doi "https://doi.org/10.1091/mbc.2.11.951" @default.
• W2108674983 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/361893" @default.
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