Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin.
A small number of proteins becomes tyrosine-phosphorylated in response to integrin-mediated cell adhesion to extracellular matrix proteins. Previous work has identified two of these tyrosine-phosphorylated proteins as the focal adhesion kinase and paxillin. Here we identify a third focal adhesion protein, tensin, that becomes tyrosine-phosphorylated during cell adhesion to extracellular matrix proteins. The tyrosine phosphorylation of tensin does not occur when cells adhere to plastic or polylysine and is blocked when microfilament assembly and cell spreading are inhibited with cytochalasin D. In addition, we show that other focal adhesion proteins such as talin and vinculin do not become tyrosine-phosphorylated under the same conditions of cell spreading on extracellular matrix proteins.
Bockholt
S M
SM
Department of Cell Biology and Anatomy, University of North Carolina, Chapel Hill 27599-7090.
Burridge
K
K
D000818:Animals; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D002465:Cell Movement / Q000187:drug effects; D002478:Cells, Cultured; D015638:Cytochalasin D / Q000494:pharmacology; D005353:Fibronectins / Q000378:metabolism*; D007797:Laminin / Q000378:metabolism*; D008840:Microfilament Proteins / Q000378:metabolism*; D010766:Phosphorylation; D051381:Rats; D000070876:Tensins; D014443:Tyrosine / Q000378:metabolism*
D015815:Cell Adhesion Molecules; D005353:Fibronectins; D007797:Laminin; D008840:Microfilament Proteins; D000070876:Tensins; C000603372:Tns1 protein, rat; D015638:Cytochalasin D; D014443:Tyrosine