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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 |
1990-2-23
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pubmed:abstractText |
Epidermal growth factor (EGF) treatment of NIH 3T3 cells transfected with wild-type EGF receptor induced tyrosine phosphorylation of phospholipase C-gamma (PLC-gamma). The EGF receptor and PLC-gamma were found to be physically associated such that antibodies directed against PLC-gamma or the EGF receptor coimmunoprecipitated both proteins. The association between PLC-gamma and wild-type EGF receptor was dependent on the concentration of EGF, but EGF did not enhance the association between PLC-gamma and a kinase-negative mutant of the EGF receptor. Oligomerization of the EGF receptor was not sufficient to induce association of the EGF receptor with PLC-gamma, since the kinase-negative mutant receptor underwent normal dimerization in response to EGF yet did not associate with PLC-gamma. The form of PLC-gamma associated with the EGF receptor appeared to be primarily the non-tyrosine-phosphorylated form. It is concluded that the kinase activity of the EGF receptor is essential for association of PLC-gamma with the EGF receptor, possibly by stimulating receptor autophosphorylation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-16068160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2433285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2457254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2459119,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2463476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2466293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2472218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2472219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2475255,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2537660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2541501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2543678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2555162,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2732223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2824188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-2915986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3017977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3023396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3075366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3181128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3257758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3259577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3260862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3263271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3499230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-3501826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-6090945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-6101263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-6277923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-6321473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2153914-6321474
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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 |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
435-41
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2153914-Animals,
pubmed-meshheading:2153914-Cells, Cultured,
pubmed-meshheading:2153914-Epidermal Growth Factor,
pubmed-meshheading:2153914-Gene Expression,
pubmed-meshheading:2153914-Genes,
pubmed-meshheading:2153914-Humans,
pubmed-meshheading:2153914-Kinetics,
pubmed-meshheading:2153914-Mice,
pubmed-meshheading:2153914-Mice, Inbred Strains,
pubmed-meshheading:2153914-Mutation,
pubmed-meshheading:2153914-Phosphorylation,
pubmed-meshheading:2153914-Protein-Tyrosine Kinases,
pubmed-meshheading:2153914-Receptor, Epidermal Growth Factor,
pubmed-meshheading:2153914-Transfection,
pubmed-meshheading:2153914-Type C Phospholipases
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pubmed:year |
1990
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pubmed:articleTitle |
Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.
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pubmed:affiliation |
Rorer Biotechnology, Inc., King of Prussia, Pennsylvania 19406.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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