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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5147
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pubmed:dateCreated |
1994-3-10
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pubmed:abstractText |
Human platelet-derived growth factor receptors (PDGFRs) expressed in human Hep G2 cells internalized and concentrated in a juxtanuclear region near the Golgi network within 10 minutes after the cells were treated with PDGF. A PDGFR mutant (F5) that lacks high-affinity binding sites for the Src homology 2 domain-containing proteins phosphatidylinositol-3 kinase (PI-3 kinase), Ras guanosine triphosphatase activating protein, phospholipase C-gamma, and a phosphotyrosine phosphatase (Syp) remained at the cell periphery. Restoration of the PI-3 kinase binding sites on F5 completely restored the ability of the receptor to concentrate intracellularly. A PDGFR mutant lacking only PI-3 kinase binding sites failed to concentrate intracellularly. Thus, PI-3 kinase binding sites appear both necessary and sufficient for the normal endocytic trafficking of the activated PDGFR.
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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/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PTPN6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet-Derived Growth Factor,
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/Receptors, Platelet-Derived Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0036-8075
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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 |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
684-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8303278-Binding Sites,
pubmed-meshheading:8303278-Cell Membrane,
pubmed-meshheading:8303278-Endocytosis,
pubmed-meshheading:8303278-GTPase-Activating Proteins,
pubmed-meshheading:8303278-Golgi Apparatus,
pubmed-meshheading:8303278-Humans,
pubmed-meshheading:8303278-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:8303278-Isoenzymes,
pubmed-meshheading:8303278-Mutation,
pubmed-meshheading:8303278-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:8303278-Phospholipase C gamma,
pubmed-meshheading:8303278-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:8303278-Platelet-Derived Growth Factor,
pubmed-meshheading:8303278-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:8303278-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:8303278-Protein Tyrosine Phosphatases,
pubmed-meshheading:8303278-Proteins,
pubmed-meshheading:8303278-Receptors, Platelet-Derived Growth Factor,
pubmed-meshheading:8303278-Tumor Cells, Cultured,
pubmed-meshheading:8303278-Type C Phospholipases,
pubmed-meshheading:8303278-ras GTPase-Activating Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites.
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pubmed:affiliation |
Program in Molecular Medicine, University of Massachusetts Medical School, Worcester 01605.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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