Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1995 May;15(5):2635-45.
doi: 10.1128/MCB.15.5.2635.

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

M D Schaller  1 , J T Parsons
Affiliations

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

M D Schaller et al. Mol Cell Biol. 1995 May.

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.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Gene. 1988 Jul 15;67(1):31-40 - PubMed
    1. Mol Cell Biol. 1993 Aug;13(8):4648-56 - PubMed
    1. J Cell Biol. 1989 Jun;108(6):2401-8 - PubMed
    1. J Cell Biol. 1993 Nov;123(4):993-1005 - PubMed
    1. Mol Cell Biol. 1993 Feb;13(2):785-91 - PubMed

Publication types

MeSH terms

LinkOut - more resources