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Molecular & Cellular Proteomics 5:1359-1367, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Functional Proteomics Identifies Protein-tyrosine Phosphatase 1B as a Target of RhoA Signaling^*,S

Yukihito Kabuyama^,,¶, Stephen J. Langer^||, Kirsi Polvinen^,,**, Yoshimi Homma, Katheryn A. Resing and Natalie G. Ahn^,,

From the Departments of Chemistry and Biochemistry and ^|| Molecular, Cellular, and Developmental Biology and Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado 80309-0215 and Department of Biomolecular Sciences, Fukushima Medical University School of Medicine, Fukushima 960-1295, Japan

Rho GTPases are signal transduction effectors that control cell motility, cell attachment, and cell shape by the control of actin polymerization and tyrosine phosphorylation. To identify cellular targets regulated by Rho GTPases, we screened global protein responses to Rac1, Cdc42, and RhoA activation by two-dimensional gel electrophoresis and mass spectrometry. A total of 22 targets were identified of which 19 had never been previously linked to Rho GTPase pathways, providing novel insight into pathway function. One novel target of RhoA was protein-tyrosine phosphatase 1B (PTP1B), which catalyzes dephosphorylation of key signaling molecules in response to activation of diverse pathways. Subsequent analysis demonstrated that RhoA enhances post-translational modification of PTP1B, inactivates phosphotyrosine phosphatase activity, and up-regulates tyrosine phosphorylation of p130Cas, a key mediator of focal adhesion turnover and cell migration. Thus, protein profiling reveals a novel role for PTP1B as a mediator of RhoA-dependent phosphorylation of p130Cas.

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