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PMID: 7537852 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk.

Molecular and cellular biology ·Vol. 15 ·No. 5 ·1995-05-00 ·Pages 2635-45

Schaller MD, Parsons JT

Abstract

Paxillin, a focal-adhesion-associated protein, becomes phosphorylated in response to a number of stimuli which also induce the tyrosine phosphorylation of the focal-adhesion-associated protein tyrosine kinase pp125FAK. On the basis of their colocalization and coordinate phosphorylation, paxillin is a candidate for a substrate of pp125FAK. We describe here conditions under which the phosphorylation of paxillin on tyrosine is pp125FAK dependent, supporting the hypothesis that paxillin phosphorylation is regulated by pp125FAK. pp125FAK must localize to focal adhesions and become autophosphorylated to induce paxillin phosphorylation. Phosphorylation of paxillin on tyrosine creates binding sites for the SH2 domains of Crk, Csk, and Src. We identify two sites of phosphorylation as tyrosine residues 31 and 118, each of which conforms to the Crk SH2 domain binding motif, (P)YXXP. These observations suggest that paxillin serves as an adapter protein, similar to insulin receptor substrate 1, and that pp125FAK may regulate the formation of signaling complexes by directing the phosphorylation of paxillin on tyrosine.

MeSH Terms
Amino Acid Sequence Animals Binding Sites/genetics Cell Adhesion Molecules/chemistry,metabolism Chick Embryo Cytoskeletal Proteins/chemistry,genetics,metabolism Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Models, Molecular Molecular Sequence Data Oncogene Protein v-crk Paxillin Peptides/genetics,metabolism Phosphoproteins/chemistry,genetics,metabolism Phosphorylation Protein Binding Protein-Tyrosine Kinases/chemistry,metabolism Proto-Oncogene Proteins pp60(c-src)/chemistry,metabolism Retroviridae Proteins, Oncogenic/chemistry,genetics,metabolism Substrate Specificity Tyrosine/metabolism
Chemicals
Cell Adhesion Molecules Cytoskeletal Proteins Oncogene Protein v-crk Paxillin Peptides Phosphoproteins Retroviridae Proteins, Oncogenic Tyrosine Protein-Tyrosine Kinases Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Proto-Oncogene Proteins pp60(c-src)
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Schaller M D
Department of Microbiology, University of Virginia, Charlottesville 22908, USA.
Parsons J T
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1995-05-00
Pages
2635-45
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC230493
Subset
IM
Grants
NCI NIH HHS · CA 40042 · United States
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