Journal
FEBS LETTERS
Volume 506, Issue 3, Pages 207-210Publisher
WILEY
DOI: 10.1016/S0014-5793(01)02912-X
Keywords
CD157; focal adhesion kinase; localization; morphology; proliferation; tyrosine phosphorylation
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CD157, a glycosylphosphatidylinositol-anchored protein, has previously been shown to mediate tyrosine phosphorylation of a 130 kDa protein (p130) in several cell lines. In this study, we have identified the p130 protein to be focal adhesion kinase (FAK or pp125(FAK)). FAK undergoes phosphorylation at Tyr-397 and Tyr-861 in intact MCA102 cells stably transfected with CD157 (MCA/CD157). MCA/CD157 cells, which displayed a rounded and compact cell morphology, exhibited a dispersed distribution, in contrast to a more closely associated and elongated spindle cell shape in the vector-transfected cells. MCA/CD157 cells proliferated at a rate 20-25% slower than the control cells. Our results demonstrate, for the first time, that FAK is a downstream signalling molecule of CD157. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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