Premium
Signalling of GPI‐anchored CD157 via focal adhesion kinase in MCA102 fibroblasts
Author(s) -
Liang Fubo,
Chang Chan Fong
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02912-x
Subject(s) - focal adhesion , transfection , phosphorylation , microbiology and biotechnology , kinase , ptk2 , adhesion , cell adhesion , tyrosine kinase , tyrosine phosphorylation , cell , chemistry , cell culture , protein kinase a , signal transduction , biology , biochemistry , mitogen activated protein kinase kinase , genetics , organic chemistry
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.