| http://purl.uniprot.org/citations/23901139 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23901139 | http://www.w3.org/2000/01/rdf-schema#comment | "Phosphatidylcholine transfer protein (PC-TP) is a phospholipid-binding protein that is enriched in liver and that interacts with thioesterase superfamily member 2 (THEM2). Mice lacking either protein exhibit improved hepatic glucose homeostasis and are resistant to diet-induced diabetes. Insulin receptor substrate 2 (IRS2) and mammalian target of rapamycin complex 1 (mTORC1) are key effectors of insulin signaling, which is attenuated in diabetes. We found that PC-TP inhibited IRS2, as evidenced by insulin-independent IRS2 activation after knockdown, genetic ablation, or chemical inhibition of PC-TP. In addition, IRS2 was activated after knockdown of THEM2, providing support for a role for the interaction of PC-TP with THEM2 in suppressing insulin signaling. Additionally, we showed that PC-TP bound to tuberous sclerosis complex 2 (TSC2) and stabilized the components of the TSC1-TSC2 complex, which functions to inhibit mTORC1. Preventing phosphatidylcholine from binding to PC-TP disrupted interactions of PC-TP with THEM2 and TSC2, and disruption of the PC-TP-THEM2 complex was associated with increased activation of both IRS2 and mTORC1. In livers of mice with genetic ablation of PC-TP or that had been treated with a PC-TP inhibitor, steady-state amounts of IRS2 were increased, whereas those of TSC2 were decreased. These findings reveal a phospholipid-dependent mechanism that suppresses insulin signaling downstream of its receptor."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.org/dc/terms/identifier | "doi:10.1126/scisignal.2004111"xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "White M.F."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "Cohen D.E."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "Ukomadu C."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "Manning B.D."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "Michel T."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "Ersoy B.A."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "D'Aquino K."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "Hancer N.J."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/author | "Tarun A."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/name | "Sci Signal"xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/pages | "ra64"xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/title | "Phosphatidylcholine transfer protein interacts with thioesterase superfamily member 2 to attenuate insulin signaling."xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://purl.uniprot.org/core/volume | "6"xsd:string |
| http://purl.uniprot.org/citations/23901139 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23901139 |
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