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• W1926397135 startingPage "785" @default.
• W1926397135 abstract "Integrins play a central role in cellular adhesion and anchorage of the cytoskeleton and participate in the generation of intracellular signals, including tyrosine phosphorylation. We have recently isolated a cDNA encoding a unique, focal adhesion-associated protein tyrosine kinase (FAK) that is a component of an integrin-mediated signal transduction pathway. Here we report the isolation of cDNAs encoding the C-terminal, noncatalytic domain of the FAK kinase, termed FRNK (FAK-related nonkinase). Both the FAK- and FRNK-encoded polypeptides, pp125FAK and p41/p43FRNK, are expressed in normal chicken embryo cells. pp125FAK and p41/p43FRNK were localized to focal adhesions, suggesting that pp125FAK is directed to the focal adhesions by sequences within its C-terminal domain. We also show that the fibronectin-dependent increase in tyrosine phosphorylation of pp125FAK is accompanied by a concomitant posttranslational modification of p41FRNK." @default.
• W1926397135 created "2016-06-24" @default.
• W1926397135 creator A5051634622 @default.
• W1926397135 creator A5054225066 @default.
• W1926397135 creator A5068938871 @default.
• W1926397135 date "1993-02-01" @default.
• W1926397135 modified "2023-09-26" @default.
• W1926397135 title "Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK" @default.
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• W1926397135 doi "https://doi.org/10.1128/mcb.13.2.785-791.1993" @default.
• W1926397135 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/358961" @default.
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