Source:http://linkedlifedata.com/resource/pubmed/id/11235915
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2001-3-8
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pubmed:abstractText |
To identify proteins interacting in the insulin-signaling pathway that might define new pathways or regulate existing ones, we have employed the yeast two-hybrid system. In a two-hybrid screen of a human liver cDNA library, we identified the human growth factor receptor bound 14 (hGrb14) adaptor protein as a partner of the activated insulin receptor. Additional analysis of the insulin receptor--hGrb14 interaction in the yeast two-hybrid system revealed that the SH2 domain of hGrb14 was not the sole region involved in binding the activated insulin receptor. The insulin-stimulated interaction between hGrb14 and the insulin receptor was also observed in different mammalian cultured cell lines. This association was detected at 1 min of insulin stimulation and was maximal at 10 nM and greater concentrations of insulin. Chinese hamster ovary cells stably expressing the insulin receptor (CHO-IR) and hGrb14 were used to examine the effects of hGrb14 overexpression on insulin-stimulated tyrosine phosphorylation of proteins; in general, increasing levels of hGrb14 expression resulted in a reduction in tyrosine phosphorylation. This decrease was demonstrated for the specific proteins src homology-containing and collagen-related protein (Shc), insulin receptor substrate-1 (IRS-1), and Downstream of tyrosine Kinase (Dok). The broad effects of hGrb14 overexpression on insulin-stimulated tyrosine phosphorylation suggest that it acts early in the insulin-signaling pathway.
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pubmed:language |
eng
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pubmed:journal | |
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/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/GRB14 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin
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pubmed:status |
MEDLINE
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pubmed:issn |
0829-8211
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
79
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21-32
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11235915-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11235915-Animals,
pubmed-meshheading:11235915-Base Sequence,
pubmed-meshheading:11235915-CHO Cells,
pubmed-meshheading:11235915-Cricetinae,
pubmed-meshheading:11235915-Cytoplasm,
pubmed-meshheading:11235915-DNA Primers,
pubmed-meshheading:11235915-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11235915-Humans,
pubmed-meshheading:11235915-Insulin,
pubmed-meshheading:11235915-Phosphorylation,
pubmed-meshheading:11235915-Protein Binding,
pubmed-meshheading:11235915-Proteins,
pubmed-meshheading:11235915-Receptor, Insulin,
pubmed-meshheading:11235915-Signal Transduction
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pubmed:year |
2001
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pubmed:articleTitle |
Human growth factor receptor bound 14 binds the activated insulin receptor and alters the insulin-stimulated tyrosine phosphorylation levels of multiple proteins.
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pubmed:affiliation |
Department of Biochemistry & Medical Genetics, University of Manitoba, Winnipeg, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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