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Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase

JD Hildebrand, MD Schaller and JT Parsons

Department of Microbiology, University of Virginia, Charlottesville 22908, USA.

Focal adhesion kinase (pp125FAK or FAK) and paxillin colocalize with integrins in structures called focal adhesions. pp125FAK plays an important role in the transmission of integrin-induced cytoplasmic signals. Paxillin has also been implicated in cell signaling by virtue of its association with the protein tyrosine kinases pp60src and Csk (C- terminal Src kinase) as well as with the adapter/oncoprotein p47gag- crk. In this report we show that endogenous pp125FAK and paxillin form a stable complex both in vivo and in vitro and that this interaction is direct, requiring only pp125FAK and paxillin. The paxillin binding site on pp125FAK has been localized to the carboxy-terminal 148 residues of pp125FAK, but appears to be distinct from the previously identified focal adhesion-targeting sequence also present in the carboxy-terminal domain of pp125FAK. The interaction of paxillin and pp125FAK is independent of the adhesion of cells to the extracellular matrix, as the association can be detected in suspension cells as well as those attached to fibronectin.

Volume 6, Issue 6, pp. 637-647, 06/01/1995
Copyright © 1995 by The American Society for Cell Biology




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HypertensionHome page
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H. L. Ostergaard, O. Lou, C. W. Arendt, and N. N. Berg
Paxillin Phosphorylation and Association with Lck and Pyk2 in Anti-CD3- or Anti-CD45-stimulated T Cells
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B. Levkau, B. Herren, H. Koyama, R. Ross, and E. W. Raines
Caspase-mediated Cleavage of Focal Adhesion Kinase pp125FAK and Disassembly of Focal Adhesions in Human Endothelial Cell Apoptosis
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SH2- and SH3-mediated Interactions between Focal Adhesion Kinase and Src
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M. P. Lutz, A. Piiper, H. Y. Gaisano, D. Stryjek-Kaminska, S. Zeuzem, and G. Adler
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W.-c. Xiong and J. T. Parsons
Induction of Apoptosis after Expression of PYK2, a Tyrosine Kinase Structurally Related to Focal Adhesion Kinase
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Integrin-mediated Activation of Focal Adhesion Kinase Is Independent of Focal Adhesion Formation or Integrin Activation. STUDIES WITH ACTIVATED AND INHIBITORY beta 3 CYTOPLASMIC DOMAIN MUTANTS
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X. Li and H. S. Earp
Paxillin Is Tyrosine-phosphorylated by and Preferentially Associates with the Calcium-dependent Tyrosine Kinase in Rat Liver Epithelial Cells
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T. H. Lin, A. E. Aplin, Y. Shen, Q. Chen, M. Schaller, L. Romer, I. Aukhil, and R.L. Juliano
Integrin-mediated Activation of MAP Kinase Is Independent of FAK: Evidence for Dual Integrin Signaling Pathways in Fibroblasts
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Monocyte Cells and Cancer Cells Express Novel Paxillin Isoforms with Different Binding Properties to Focal Adhesion Proteins
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Complexes of Focal Adhesion Kinase (FAK) and Crk-associated Substrate (p130Cas) Are Elevated in Cytoskeleton-associated Fractions following Adhesion and Src Transformation. REQUIREMENTS FOR Src KINASE ACTIVITY AND FAK PROLINE-RICH MOTIFS
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N. Konstantopoulos and S. Clark
Reduced Cell Attachment and Phosphorylation of Focal Adhesion Kinase Associated with Expression of a Mutant Insulin Receptor
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The CRKL Adaptor Protein Transforms Fibroblasts and Functions in Transformation by the BCR-ABL Oncogene
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M. T. Harte, J. D. Hildebrand, M. R. Burnham, A. H. Bouton, and J. T. Parsons
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Requirement for Phosphatidylinositol 3`-Kinase Activity in Platelet-derived Growth Factor-stimulated Tyrosine Phosphorylation of p125 Focal Adhesion Kinase and Paxillin
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L Hemmings, D. Rees, V Ohanian, S. Bolton, A. Gilmore, B Patel, H Priddle, J. Trevithick, R. Hynes, and D. Critchley
Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site
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