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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1995-6-12
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pubmed:abstractText |
The focal adhesion kinase, pp125FAK, is a novel non-receptor protein tyrosine kinase expressed in different cells including mast cells. Here we report that a 77-kDa protein associates with pp125FAK in the mast cell analog, rat basophilic leukemia (RBL-2H3) cells. When pp125FAK immunoprecipitates were subjected to an in vitro kinase assay, there was prominent phosphorylation on tyrosine of pp125FAK and of a 77-kDa protein. By V8 protease digestion mapping and by immunoblotting with two different anti-pp125FAK antibodies, the 77-kDa protein was distinct from pp125FAK. This Fak Associated Protein or FAP was detected in RBL-2H3 cells but not in fibroblasts. The aggregation of the high affinity IgE receptor, Fc epsilon RI, induced the in vivo tyrosine phosphorylation of FAP. However, there was a marked decrease in the in vitro phosphorylation of FAP in the immunoprecipitates from Fc epsilon RI aggregated cells. Both of these Fc epsilon RI-mediated effects were enhanced by cell adhesion. There was strong association of FAP with non-tyrosine-phosphorylated pp125FAK. Thus this interaction does not appear to be mediated by the Src homology 2 domain. Together the data indicate that FAP associates with pp125FAK and suggest that FAP may play a role in Fc epsilon RI signaling.
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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/Focal Adhesion Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Protein-Tyrosine...,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin E,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptk2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptk2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgE
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pubmed:status |
MEDLINE
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pubmed:month |
May
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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 |
19
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12305-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7744883-3T3 Cells,
pubmed-meshheading:7744883-Animals,
pubmed-meshheading:7744883-Cell Adhesion Molecules,
pubmed-meshheading:7744883-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:7744883-Focal Adhesion Kinase 1,
pubmed-meshheading:7744883-Focal Adhesion Protein-Tyrosine Kinases,
pubmed-meshheading:7744883-Immunoglobulin E,
pubmed-meshheading:7744883-Immunologic Capping,
pubmed-meshheading:7744883-Leukemia, Basophilic, Acute,
pubmed-meshheading:7744883-Mast Cells,
pubmed-meshheading:7744883-Mice,
pubmed-meshheading:7744883-Neoplasm Proteins,
pubmed-meshheading:7744883-Phosphorylation,
pubmed-meshheading:7744883-Protein Processing, Post-Translational,
pubmed-meshheading:7744883-Protein-Tyrosine Kinases,
pubmed-meshheading:7744883-Rats,
pubmed-meshheading:7744883-Receptors, IgE,
pubmed-meshheading:7744883-Tumor Cells, Cultured
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pubmed:year |
1995
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pubmed:articleTitle |
A 77-kDa protein associates with pp125FAK in mast cells and becomes tyrosine-phosphorylated by high affinity IgE receptor aggregation.
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pubmed:affiliation |
Laboratory of Immunology, NIDR, National Institutes of Health, Bethesda, Maryland 20892-1188, USA.
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pubmed:publicationType |
Journal Article
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