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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1999-4-27
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pubmed:databankReference |
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pubmed:abstractText |
Transmembrane ephrinB proteins have important functions during embryonic patterning as ligands for Eph receptor tyrosine kinases and presumably as signal-transducing receptor-like molecules. Consistent with "reverse" signaling, ephrinB1 is localized in sphingo-lipid/cholesterol-enriched raft microdomains, platforms for the localized concentration and activation of signaling molecules. Glutamate receptor-interacting protein (GRIP) and a highly related protein, which we have termed GRIP2, are recruited into these rafts through association with the C-terminal PDZ target site of ephrinB1. Stimulation of ephrinB1 with soluble EphB2 receptor ectodomain causes the formation of large raft patches that also contain GRIP proteins. Moreover, a GRIP-associated serine/threonine kinase activity is recruited into ephrinB1-GRIP complexes. Our findings suggest that GRIP proteins provide a scaffold for the assembly of a multiprotein signaling complex downstream of ephrinB ligands.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-B1,
http://linkedlifedata.com/resource/pubmed/chemical/Grip1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Grip1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Grip2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoamino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
511-24
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10197531-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10197531-Amino Acid Sequence,
pubmed-meshheading:10197531-Animals,
pubmed-meshheading:10197531-Blotting, Western,
pubmed-meshheading:10197531-Brain,
pubmed-meshheading:10197531-Carrier Proteins,
pubmed-meshheading:10197531-Cell Line,
pubmed-meshheading:10197531-Cell Membrane,
pubmed-meshheading:10197531-Ephrin-B1,
pubmed-meshheading:10197531-Gene Deletion,
pubmed-meshheading:10197531-In Situ Hybridization,
pubmed-meshheading:10197531-Ligands,
pubmed-meshheading:10197531-Membrane Proteins,
pubmed-meshheading:10197531-Mice,
pubmed-meshheading:10197531-Molecular Sequence Data,
pubmed-meshheading:10197531-Nerve Tissue Proteins,
pubmed-meshheading:10197531-Neurons,
pubmed-meshheading:10197531-Organ Specificity,
pubmed-meshheading:10197531-Phosphoamino Acids,
pubmed-meshheading:10197531-Precipitin Tests,
pubmed-meshheading:10197531-Protein-Serine-Threonine Kinases,
pubmed-meshheading:10197531-Rats
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pubmed:year |
1999
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pubmed:articleTitle |
EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains.
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pubmed:affiliation |
Developmental Biology Programme, European Molecular Biology Laboratory, Heidelberg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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