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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1998-4-7
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pubmed:abstractText |
Tyrosine phosphorylation of focal adhesion-associated proteins may be involved in the regulation of the cytoskeleton and in the control of signals for growth and survival. The focal adhesion kinase (FAK) functions in regulating tyrosine phosphorylation of several of these proteins, including paxillin, tensin, and p130(cas). Protein- tyrosine phosphatases, the counterparts of protein-tyrosine kinases, also presumably regulate phosphorylation of these proteins. We have tested the hypothesis that FAK intimately associates with a protein-tyrosine phosphatase. Protein-tyrosine phosphatase activity associated with the recombinant C-terminal domain of FAK in vitro and could be coimmunoprecipitated with both FAK and paxillin from lysates of chicken embryo cells. However, the interaction with FAK appeared to be indirect and mediated via paxillin. The protein-tyrosine phosphatase was subsequently identified as protein-tyrosine phosphatase-PEST, a nonreceptor protein-tyrosine phosphatase. The C-terminal noncatalytic domain of protein-tyrosine phosphatase-PEST directly bound to paxillin in vitro. The association of both a protein-tyrosine kinase and a protein-tyrosine phosphatase with paxillin suggests that paxillin may play a critical role in the regulation of the phosphotyrosine content of proteins in focal adhesions.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Protein-Tyrosine...,
http://linkedlifedata.com/resource/pubmed/chemical/Paxillin,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptk2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn12 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Pxn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6474-81
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9497381-3T3 Cells,
pubmed-meshheading:9497381-Animals,
pubmed-meshheading:9497381-Binding Sites,
pubmed-meshheading:9497381-COS Cells,
pubmed-meshheading:9497381-Cell Adhesion,
pubmed-meshheading:9497381-Cell Adhesion Molecules,
pubmed-meshheading:9497381-Chick Embryo,
pubmed-meshheading:9497381-Cytoskeletal Proteins,
pubmed-meshheading:9497381-Focal Adhesion Kinase 1,
pubmed-meshheading:9497381-Focal Adhesion Protein-Tyrosine Kinases,
pubmed-meshheading:9497381-Mice,
pubmed-meshheading:9497381-Models, Biological,
pubmed-meshheading:9497381-Paxillin,
pubmed-meshheading:9497381-Phosphoproteins,
pubmed-meshheading:9497381-Precipitin Tests,
pubmed-meshheading:9497381-Protein Binding,
pubmed-meshheading:9497381-Protein Tyrosine Phosphatase, Non-Receptor Type 12,
pubmed-meshheading:9497381-Protein Tyrosine Phosphatases,
pubmed-meshheading:9497381-Protein-Tyrosine Kinases,
pubmed-meshheading:9497381-Recombinant Proteins,
pubmed-meshheading:9497381-Signal Transduction
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pubmed:year |
1998
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pubmed:articleTitle |
Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin.
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pubmed:affiliation |
Department of Cell Biology and Anatomy, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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