Sm. Bockholt et K. Burridge, CELL SPREADING ON EXTRACELLULAR-MATRIX PROTEINS INDUCES TYROSINE PHOSPHORYLATION OF TENSIN, The Journal of biological chemistry, 268(20), 1993, pp. 4565-4567
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 prot
eins as the focal adhesion kinase and paxillin. Here we identify a thi
rd focal adhesion protein, tensin, that becomes tyrosine-phosphorylate
d 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 spre
ading are inhibited with cytochalasin D. In addition, we show that oth
er focal adhesion proteins such as talin and vinculin do not become ty
rosine-phosphorylated under the same conditions of cell spreading on e
xtracellular matrix proteins.