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W2010087461 startingPage "15174" @default.
W2010087461 abstract "The product of the c- abl protooncogene is a nonreceptor tyrosine kinase found in both the cytoplasm and the nucleus. We report herein that cell adhesion regulates the kinase activity and subcellular localization of c-Abl. When fibroblastic cells are detached from the extracellular matrix, kinase activity of both cytoplasmic and nuclear c-Abl decreases, but there is no detectable alteration in the subcellular distribution. Upon adhesion to the extracellular matrix protein fibronectin, a transient recruitment of a subset of c-Abl to early focal contacts is observed coincident with the export of c-Abl from the nucleus to the cytoplasm. The cytoplasmic pool of c-Abl is reactivated within 5 min of adhesion, but the nuclear c-Abl is reactivated after 30 min, correlating closely with its return to the nucleus and suggesting that the active nuclear c-Abl originates in the cytoplasm. In quiescent cells where nuclear c-Abl activity is low, the cytoplasmic c-Abl is similarly regulated by adhesion but the nuclear c-Abl is not activated upon cell attachment. These results show that c-Abl activation requires cell adhesion and that this tyrosine kinase can transmit integrin signals to the nucleus where it may function to integrate adhesion and cell cycle signals." @default.
W2010087461 created "2016-06-24" @default.
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W2010087461 date "1996-12-24" @default.
W2010087461 modified "2023-10-18" @default.
W2010087461 title "Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic–nuclear transport" @default.
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W2010087461 doi "https://doi.org/10.1073/pnas.93.26.15174" @default.
W2010087461 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/26376" @default.
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