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- W2000983089 endingPage "1005" @default.
- W2000983089 startingPage "993" @default.
- W2000983089 abstract "The integrin family of heterodimeric cell surface receptors play critical roles in multiple biological processes by mediating cellular adhesion to the extracellular matrix (ECM). Adhesion triggers intracellular signaling cascades, including tyrosine phosphorylation and elevation of [Ca2+]i. The Focal Adhesion Kinase (FAK or pp125FAK), a protein tyrosine kinase that colocalizes with integrins in cellular focal adhesions, is a prime candidate for a mediator of integrin signaling events. Here we report an analysis of the domain structure of FAK in which we have identified a contiguous stretch of 159 amino acids within the COOH terminus essential for correct subcellular localization. When placed in the context of an unrelated cytosolic protein, this Focal Adhesion Targeting (FAT) sequence functions to efficiently mediate the focal adhesion localization of this fusion protein. Furthermore, this analysis suggests that pp125FAK cannot be activated oncogenically by mutation. This result could be explained if pp125FK either exhibits a narrow substrate specificity or is diametrically opposed by cellular phosphatases or other cellular processes." @default.
- W2000983089 created "2016-06-24" @default.
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- W2000983089 creator A5049924632 @default.
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- W2000983089 date "1993-11-15" @default.
- W2000983089 modified "2023-09-26" @default.
- W2000983089 title "Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions." @default.
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- W2000983089 doi "https://doi.org/10.1083/jcb.123.4.993" @default.
- W2000983089 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2200138" @default.
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