Focal Adhesion Kinase (P125FAK) and Paxillin Are Substrates for Sphingomyelinase-Induced Tyrosine Phosphorylation in Swiss 3T3 Fibroblasts

Biochemical Journal- United Kingdom

doi 10.1042/bj3151035

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May 1, 1996

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Portland Press Ltd.

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Focal Adhesion Kinase (P125FAK) and Paxillin Are Substrates for Sphingomyelinase-Induced Tyrosine Phosphorylation in Swiss 3T3 Fibroblasts

Biochemical Journal- United Kingdom

Full Text

Abstract

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Date

Authors

Publisher

Related search

Rho-Dependent and -Independent Tyrosine Phosphorylation of Focal Adhesion Kinase, Paxillin and P130Cas Mediated by Ret Kinase

Insulin-Like Growth Factor I Stimulates Tyrosine Phosphorylation of P130Cas, Focal Adhesion Kinase, and Paxillin

Requirement for Phosphatidylinositol 3′-Kinase Activity in Platelet-Derived Growth Factor-Stimulated Tyrosine Phosphorylation of P125 Focal Adhesion Kinase and Paxillin

The Related Adhesion Focal Tyrosine Kinase Forms a Complex With Paxillin in Hematopoietic Cells

The Focal Adhesion Kinase (P125FAK) Is Constitutively Active in Human Malignant Melanoma

Selected Contribution: Skeletal Muscle Focal Adhesion Kinase, Paxillin, and Serum Response Factor Are Loading Dependent

Effect of Tumor Gangliosides on Tyrosine Phosphorylation of P125FAK in Platelet Adhesion to Collagen

In Vitro Phosphorylation of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase by SRC Kinase

Association of Β1 Integrin With Focal Adhesion Kinase and Paxillin in Differentiating Schwann Cells