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Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase

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 reac...

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Published in:The Journal of biological chemistry 1992-11, Vol.267 (33), p.23439-23442
Main Authors: KORNBERG, L, SHELTON EARP, H, THOMAS PARSONS, J, SCHALLER, M, JULIANO, R. L
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container_issue 33
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description 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.
doi_str_mv 10.1016/s0021-9258(18)35853-8
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L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-11-25</date><risdate>1992</risdate><volume>267</volume><issue>33</issue><spage>23439</spage><epage>23442</epage><pages>23439-23442</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>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. 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subjects Animals
Biological and medical sciences
Blotting, Western
Cell Adhesion
Cell Adhesion Molecules - isolation & purification
Cell Adhesion Molecules - metabolism
Cell physiology
Cells, Cultured
Chick Embryo
chickens
Electrophoresis, Polyacrylamide Gel
fibroblasts
Fibroblasts - physiology
fibronectin
Fibronectins - metabolism
Focal Adhesion Kinase 1
Focal Adhesion Protein-Tyrosine Kinases
focal adhesion-associated tyrosine kinase
Fundamental and applied biological sciences. Psychology
Humans
integrin
Integrins - metabolism
KB Cells
Kinetics
mediation
Molecular and cellular biology
Molecular Weight
Phosphorylation
Protein-Tyrosine Kinases - isolation & purification
Protein-Tyrosine Kinases - metabolism
receptors
Signal Transduction
tyrosine
title Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
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