http://purl.uniprot.org/citations/21907143 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21907143 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/21907143 | http://www.w3.org/2000/01/rdf-schema#comment | "The protein kinase B(β) (Akt2) pathway is known to mediate insulin-stimulated glucose transport through increasing glucose transporter GLUT4 translocation from intracellular stores to the plasma membrane (PM). Combining quantitative phosphoproteomics with RNAi-based functional analyses, we show that a previously uncharacterized 138 kDa C2 domain-containing phosphoprotein (CDP138) is a substrate for Akt2, and is required for optimal insulin-stimulated glucose transport, GLUT4 translocation, and fusion of GLUT4 vesicles with the PM in live adipocytes. The purified C2 domain is capable of binding Ca(2+) and lipid membranes. CDP138 mutants lacking the Ca(2+)-binding sites in the C2 domain or Akt2 phosphorylation site S197 inhibit insulin-stimulated GLUT4 insertion into the PM, a rate-limiting step of GLUT4 translocation. Interestingly, CDP138 is dynamically associated with the PM and GLUT4-containing vesicles in response to insulin stimulation. Together, these results suggest that CDP138 is a key molecule linking the Akt2 pathway to the regulation of GLUT4 vesicle-PM fusion."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cmet.2011.06.015"xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cmet.2011.06.015"xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Czech M.P."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Czech M.P."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Gong Z."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Gong Z."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Kruger M."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Kruger M."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Gnad F."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Gnad F."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Mann M."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Mann M."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Xie X."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Xie X."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Jiang Z.Y."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Jiang Z.Y."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Brill L.M."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Brill L.M."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Mansuy-Aubert V."xsd:string |
http://purl.uniprot.org/citations/21907143 | http://purl.uniprot.org/core/author | "Mansuy-Aubert V."xsd:string |