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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1998-3-5
|
| pubmed:databankReference | |
| pubmed:abstractText |
Insulin receptor (IR) and the related insulin-like growth factor-I (IGF-I) receptor (IGF-IR) mediate a variety of metabolic and mitogenic cellular responses, some of which may involve unidentified receptor targets. A Src homology-2 (SH2) domain-coding region of a mouse protein was cloned based on its interaction with IR. It was designated mSH2-B based on its high similarity to an earlier reported rat sequence SH2-B. A role of mSH2-B in IGF-I and insulin action was suggested by the interaction of the SH2 domain with activated IGF-IR and IR catalytic fragments but not with an inactive IR catalytic fragment in the yeast two-hybrid system in vivo and by the hormone-dependent association of a glutathione S-transferase (GST) SH2 domain fusion protein of mSH2-B with both receptors in cell extracts. A comparison of IGF-IR and IR mutants lacking individual Tyr autophosphorylation sites for association with GST mSH2-B showed that homologous juxtamembrane (IR960/IGF-IR950) and C-terminal (IR1322/IGF-IR1316) receptor motifs were required. Synthetic phosphopeptides representing IR960 and IR1322 competed for GST mSH2-B binding to the receptor, suggesting that both motifs participate in the association with mSH2-B. Antibodies raised against GST mSH2-B identified a cellular protein of 92 kDa that was not found to be phosphorylated on Tyr. It co-immunoprecipitated with IGF-IR or IR, which was strictly dependent on receptor activation. IR and IGF-IR Tyr phosphorylation motifs were not identified in the complete SH2-B primary structure, suggesting that it may participate as an adapter rather than a substrate in the IGF-I and insulin signaling pathways.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| 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/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sh2bpsm1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sh2bpsm1 protein, rat
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
6
|
| pubmed:volume |
273
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
3136-9
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9452421-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9452421-Animals,
pubmed-meshheading:9452421-CHO Cells,
pubmed-meshheading:9452421-Carrier Proteins,
pubmed-meshheading:9452421-Catalysis,
pubmed-meshheading:9452421-Cricetinae,
pubmed-meshheading:9452421-Glutathione Transferase,
pubmed-meshheading:9452421-Ligands,
pubmed-meshheading:9452421-Mice,
pubmed-meshheading:9452421-Molecular Sequence Data,
pubmed-meshheading:9452421-Phosphopeptides,
pubmed-meshheading:9452421-Phosphorylation,
pubmed-meshheading:9452421-Protein Binding,
pubmed-meshheading:9452421-Rats,
pubmed-meshheading:9452421-Receptor, IGF Type 1,
pubmed-meshheading:9452421-Receptor, Insulin,
pubmed-meshheading:9452421-Recombinant Fusion Proteins,
pubmed-meshheading:9452421-Recombinant Proteins,
pubmed-meshheading:9452421-Signal Transduction,
pubmed-meshheading:9452421-src Homology Domains
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Insulin-like growth factor-I receptor and insulin receptor association with a Src homology-2 domain-containing putative adapter.
|
| pubmed:affiliation |
Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|