Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 1993 Jul 15;268(20):14565-7.

Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin.

Author information

  • 1Department of Cell Biology and Anatomy, University of North Carolina, Chapel Hill 27599-7090.

Abstract

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.

PMID:
8325835
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for HighWire
    Loading ...
    Write to the Help Desk