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J. Biol. Chem., Vol. 267, Issue 33, 23439-23442, 11, 1992
L Kornberg, HS Earp, JT Parsons, M Schaller and RL Juliano
We have recently shown that changes in tyrosine phosphorylation of a
130-kDa protein(s) (pp130) may be involved in integrin signaling (Kornberg,
L., Earp, H.S., Turner, C., Prokop, and Juliano, R. L. (1991) Proc. Natl.
Acad. Sci. U.S.A. 88, 8392-8396). One component of the pp130 protein
complex reacts with an antibody generated against p125fak, which is a focal
contact-associated tyrosine kinase (Schaller, M.D., Borgman, C. A., Cobb,
B. S., Vines, R. R., Reynolds, A. B., and Parsons, J. T. (1992) Proc. Natl.
Acad. Sci. U.S.A. 89, 5192-5196). Both antibody-mediated integrin
clustering and adhesion of KB cells to fibronectin leads to increased
tyrosine phosphorylation of p125fak. The phosphorylation of p125fak is
coincident with adhesion of cells to fibronectin and is maximal prior to
cell spreading. Tyrosine phosphorylation of p125fak is induced when KB
cells are allowed to adhere to fibronectin, collagen type IV, or laminin,
but is not induced on polylysine. When KB cells are subjected to indirect
immunofluorescence microscopy, p125fak colocalizes with talin in focal
contacts. These data provide additional evidence that tyrosine kinases are
involved in integrin signaling.
Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
Department of Pharmacology, University of North Carolina, Chapel Hill 27599.
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