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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1991-3-4
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pubmed:abstractText |
Platelet-derived growth factor (PDGF) stimulates autophosphorylation of the PDGF receptor and association of the receptor with several cytoplasmic molecules, including phosphatidylinositol-3 kinase (PI3 kinase). In this study we examined the association of PI3 kinase with immunoprecipitated autophosphorylated PDGF receptor in vitro. The PI3 kinase from cell lysates bound to the wild-type receptor but not to a mutant receptor that had a deletion of the kinase insert region. A protein of an apparent size of 85 kDa bound to the receptor, consistent with previous observations that a protein of this size is associated with PI3 kinase activity. In addition, 110- and 74-kDa proteins bound to the phosphorylated receptor. Dephosphorylated receptors lost the ability to bind PI3 kinase activity as well as the 85-kDa protein. A 20-amino-acid peptide composed of a sequence in the kinase insert region that included one of the autophosphorylation sites of the receptor (tyrosine 719) as well as a nearby tyrosine (Y708) blocked the binding of PI3 kinase to the receptor, but only when the peptide was phosphorylated on tyrosine residues. A scrambled version of the peptide did not block PI3 kinase binding to the receptor even when it was phosphorylated on tyrosine. These tyrosine-phosphorylated peptides did not block binding of phospholipase C-gamma or GTPase-activating protein to the receptor. In separate experiments (receptor blots), soluble radiolabeled receptor bound specifically to an 85-kDa protein present in sodium dodecyl sulfate-polyacrylamide gel electrophoresis-fractionated 3T3 cell lysates that were transferred to nitrocellulose paper. The binding was blocked by the same tyrosine-phosphorylated peptides that prevented binding of PI3 kinase activity to immobilized receptors. These findings show that the PDGF receptor binds directly to an 85-kDa protein and to a PI3 kinase activity through specific sequences in the kinase insert region. The association of a 110-kDa protein with the receptor also involve these sequences, suggesting that this protein may be a subunit of the PI3 kinase. Phosphotyrosine is an essential structure required for the interactions of these proteins with the PDGF receptor.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-1691440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2140428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2156626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2157284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2160590,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2170111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2441878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2441879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2466336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2467744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2472219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2475255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2479827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2480526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2538922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2542288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2542295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2542773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2545680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2550144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2550789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2554305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2556641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2825654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2833705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2842689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2843499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-2987699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-3020426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-6203898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-6326105,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1703628-6980882
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1125-32
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1703628-Amino Acid Sequence,
pubmed-meshheading:1703628-Animals,
pubmed-meshheading:1703628-Baculoviridae,
pubmed-meshheading:1703628-Binding Sites,
pubmed-meshheading:1703628-Cell Line,
pubmed-meshheading:1703628-Insects,
pubmed-meshheading:1703628-Mice,
pubmed-meshheading:1703628-Mice, Inbred BALB C,
pubmed-meshheading:1703628-Molecular Sequence Data,
pubmed-meshheading:1703628-Molecular Weight,
pubmed-meshheading:1703628-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:1703628-Phosphopeptides,
pubmed-meshheading:1703628-Phosphotransferases,
pubmed-meshheading:1703628-Phosphotyrosine,
pubmed-meshheading:1703628-Platelet-Derived Growth Factor,
pubmed-meshheading:1703628-Receptors, Cell Surface,
pubmed-meshheading:1703628-Receptors, Platelet-Derived Growth Factor,
pubmed-meshheading:1703628-Tyrosine
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pubmed:year |
1991
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pubmed:articleTitle |
A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine.
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pubmed:affiliation |
Cardiovascular Research Institute, University of California San Francisco 94143.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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