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

Pub. Date : 1995 May

PMID : 7537852






7 Functional Relationships(s)
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Protein Name
Organism
1 pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Tyrosine paxillin Homo sapiens
2 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. Tyrosine paxillin Homo sapiens
3 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. Tyrosine paxillin Homo sapiens
4 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. Tyrosine paxillin Homo sapiens
5 Phosphorylation of paxillin on tyrosine creates binding sites for the SH2 domains of Crk, Csk, and Src. Tyrosine paxillin Homo sapiens
6 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. Tyrosine paxillin Homo sapiens
7 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. Tyrosine paxillin Homo sapiens