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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
36
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pubmed:dateCreated |
1998-10-15
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pubmed:abstractText |
Receptor tyrosine phosphorylation is crucial for signal transduction by creating high affinity binding sites for Src homology 2 domain-containing molecules. By expressing the intracellular domain of Flt-1/vascular endothelial growth factor receptor-1 in the baculosystem, we identified two major tyrosine phosphorylation sites at Tyr-1213 and Tyr-1242 and two minor tyrosine phosphorylation sites at Tyr-1327 and Tyr-1333 in this receptor. This pattern of phosphorylation of Flt-1 was also detected in vascular endothelial growth factor-stimulated cells expressing intact Flt-1. In vitro protein binding studies using synthetic peptides and immunoblotting showed that phospholipase C-gamma binds to both Y(p)1213 and Y(p)1333, whereas Grb2 and SH2-containing tyrosine protein phosphatase (SHP-2) bind to Y(p)1213, and Nck and Crk bind to Y(p)1333 in a phosphotyrosine-dependent manner. In addition, unidentified proteins with molecular masses around 74 and 27 kDa bound to Y(p)1213 and another of 75 kDa bound to Y(p)1333 in a phosphotyrosine-dependent manner. SHP-2, phospholipase C-gamma, and Grb2 could also be shown to bind to the intact Flt-1 intracellular domain. These results indicate that a spectrum of already known as well as novel phosphotyrosine-binding molecules are involved in signal transduction by Flt-1.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Grb2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn11 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SH2 Domain-Containing Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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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 |
4
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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 |
23410-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9722576-3T3 Cells,
pubmed-meshheading:9722576-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9722576-Animals,
pubmed-meshheading:9722576-Baculoviridae,
pubmed-meshheading:9722576-Binding Sites,
pubmed-meshheading:9722576-Endothelium, Vascular,
pubmed-meshheading:9722576-GRB2 Adaptor Protein,
pubmed-meshheading:9722576-Humans,
pubmed-meshheading:9722576-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9722576-Mice,
pubmed-meshheading:9722576-Models, Molecular,
pubmed-meshheading:9722576-Peptide Fragments,
pubmed-meshheading:9722576-Peptide Mapping,
pubmed-meshheading:9722576-Phosphopeptides,
pubmed-meshheading:9722576-Phosphorylation,
pubmed-meshheading:9722576-Protein Binding,
pubmed-meshheading:9722576-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:9722576-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:9722576-Protein Tyrosine Phosphatases,
pubmed-meshheading:9722576-Proteins,
pubmed-meshheading:9722576-Proto-Oncogene Proteins,
pubmed-meshheading:9722576-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:9722576-Recombinant Proteins,
pubmed-meshheading:9722576-SH2 Domain-Containing Protein Tyrosine Phosphatases,
pubmed-meshheading:9722576-Signal Transduction,
pubmed-meshheading:9722576-Swine,
pubmed-meshheading:9722576-Type C Phospholipases,
pubmed-meshheading:9722576-Tyrosine,
pubmed-meshheading:9722576-Vascular Endothelial Growth Factor Receptor-1,
pubmed-meshheading:9722576-src Homology Domains
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pubmed:year |
1998
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pubmed:articleTitle |
Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules.
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pubmed:affiliation |
Department of Medical Biochemistry and Microbiology, Uppsala University, Biomedical Center, Box 575, S-751 23 Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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