| pubmed-article:9792713 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9792713 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
| pubmed-article:9792713 | lifeskim:mentions | umls-concept:C0206131 | lld:lifeskim |
| pubmed-article:9792713 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9792713 | lifeskim:mentions | umls-concept:C0123658 | lld:lifeskim |
| pubmed-article:9792713 | lifeskim:mentions | umls-concept:C1135629 | lld:lifeskim |
| pubmed-article:9792713 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:9792713 | pubmed:issue | 45 | lld:pubmed |
| pubmed-article:9792713 | pubmed:dateCreated | 1998-12-10 | lld:pubmed |
| pubmed-article:9792713 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9792713 | pubmed:abstractText | Signaling through the insulin receptor tyrosine kinase involves its autophosphorylation in response to insulin and the subsequent tyrosine phosphorylation of substrate proteins such as insulin receptor substrate-1 (IRS-1). In basal 3T3-L1 adipocytes, IRS-1 is predominantly membrane-bound, and this localization may be important in targeting downstream signaling elements that mediate insulin action. Since IRS-1 localization to membranes may occur through its association with specific membrane proteins, a 3T3-F442A adipocyte cDNA expression library was screened with non-tyrosine-phosphorylated, baculovirus-expressed IRS-1 in order to identify potential IRS-1 receptors. A cDNA clone that encodes sigma3A, a small subunit of the AP-3 adaptor protein complex, was demonstrated to bind IRS-1 utilizing this cloning strategy. The specific interaction between IRS-1 and sigma3A was further verified by in vitro binding studies employing baculovirus-expressed IRS-1 and a glutathione S-transferase (GST)-sigma3A fusion protein. IRS-1 and sigma3A were found to co-fractionate in a detergent-resistant population of low density membranes isolated from basal 3T3-L1 adipocytes. Importantly, the addition of exogenous purified GST-sigma3A to low density membranes caused the release of virtually all of the IRS-1 bound to these membranes, while GST alone had no effect. These results are consistent with the hypothesis that sigma3A serves as an IRS-1 receptor that may dictate the subcellular localization and the signaling functions of IRS-1. | lld:pubmed |
| pubmed-article:9792713 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9792713 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9792713 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9792713 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9792713 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9792713 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9792713 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9792713 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9792713 | pubmed:author | pubmed-author:CzechM PMP | lld:pubmed |
| pubmed-article:9792713 | pubmed:author | pubmed-author:MorinMM | lld:pubmed |
| pubmed-article:9792713 | pubmed:author | pubmed-author:Heller-Harris... | lld:pubmed |
| pubmed-article:9792713 | pubmed:author | pubmed-author:VanRenterghem... | lld:pubmed |
| pubmed-article:9792713 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9792713 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:9792713 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9792713 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9792713 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9792713 | pubmed:pagination | 29942-9 | lld:pubmed |
| pubmed-article:9792713 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:9792713 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9792713 | pubmed:articleTitle | Interaction of insulin receptor substrate-1 with the sigma3A subunit of the adaptor protein complex-3 in cultured adipocytes. | lld:pubmed |
| pubmed-article:9792713 | pubmed:affiliation | Program in Molecular Medicine and the Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, Worcester, Massachusetts 01605, USA. | lld:pubmed |
| pubmed-article:9792713 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9792713 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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