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PMID: 7511377 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Paxillin: a cytoskeletal target for tyrosine kinases.

Turner CE

Abstract

Paxillin is a recently identified member of the complex of cytoskeletal proteins that is found concentrated in cultured cells and in vivo at the cytoplasmic face of regions of cell attachment to the extracellular matrix. These sites, in view of their close proximity to the extracellular matrix, are well positioned to act as signal-transducing centers to 'report on' changes in the cells, immediate environment. Recent findings indicate that such signals are in part mediated through the activation of tyrosine kinases concentrated at the sites of adhesion. Changes in the phosphotyrosine content of paxillin accompanying this elevation in kinase activity suggest that paxillin may be an important intermediary in these pathways.

MeSH Terms
Animals Cell Adhesion Cytoskeletal Proteins/metabolism Cytoskeleton/physiology Embryonic and Fetal Development/physiology Extracellular Matrix/physiology Paxillin Phosphoproteins/metabolism Phosphotyrosine Protein-Tyrosine Kinases/metabolism Signal Transduction Tyrosine/analogs & derivatives,metabolism Vinculin/metabolism
Chemicals
Cytoskeletal Proteins Paxillin Phosphoproteins Vinculin Phosphotyrosine Tyrosine Protein-Tyrosine Kinases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Turner C E
Department of Anatomy and Cell Biology, SUNY Health Science Center, Syracuse 13210.
Article Info
Journal
BioEssays : news and reviews in molecular, cellular and developmental biology
Abbr.
Bioessays
ISSN
0265-9247
Published
1994-01-00
Pages
47-52
Language
English
Region
United States
NLM ID
8510851
Subset
IM
Grants
NIGMS NIH HHS · R01 GM047607 · United States
NIGMS NIH HHS · GM47607 · United States
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