| http://purl.uniprot.org/citations/26514725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26514725 | http://www.w3.org/2000/01/rdf-schema#comment | "Insulin resistance (IR) is a metabolic disorder characterized by impaired glucose uptake in response to insulin. The current paradigm for insulin signaling centers upon the insulin receptor (InsR) and its substrate IRS1; the latter is believed to be the chief conduit for post-receptor signaling. We recently demonstrated that GIV, a Guanidine Exchange Factor (GEF) for the trimeric G protein, Gαi, is a major hierarchical conduit for the metabolic insulin response. By virtue of its ability to directly bind the InsR, IRS1 and PI3K, GIV enhances the InsR-IRS1-Akt-AS160 (RabGAP) signaling cascade and cellular glucose uptake via its GEF function. Phosphoinhibition of GIV-GEF by the fatty-acid/PKCθ pathway inhibits the cascade and impairs glucose uptake. Here we show that GIV directly and constitutively binds the exocyst complex subunit Exo-70 and also associates with GLUT4-storage vesicles (GSVs) exclusively upon insulin stimulation. Without GIV or its GEF function, membrane association of Exo-70 as well as exocytosis of GSVs in response to insulin are impaired. Thus, GIV is an essential component within the insulin signaling cascade that couples upstream signal transducers within the InsR and G-Protein signaling cascade to downstream vesicular trafficking events within the exocytic pathway. These findings suggest a role of GIV in coordinating key signaling and trafficking events of metabolic insulin response."xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2015.10.111"xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/author | "Ghosh P."xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/author | "Lopez-Sanchez I."xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/author | "Ma G.S."xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/author | "Kalogriopoulos N."xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/author | "Pedram S."xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/pages | "287-293"xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/title | "GIV/girdin binds exocyst subunit-Exo70 and regulates exocytosis of GLUT4 storage vesicles."xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://purl.uniprot.org/core/volume | "468"xsd:string |
| http://purl.uniprot.org/citations/26514725 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26514725 |
| http://purl.uniprot.org/citations/26514725 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26514725 |
| http://purl.uniprot.org/uniprot/#_B2R8H4-mappedCitation-26514725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26514725 |
| http://purl.uniprot.org/uniprot/#_B4DSN0-mappedCitation-26514725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26514725 |
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| http://purl.uniprot.org/uniprot/#_I3L2R4-mappedCitation-26514725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26514725 |
| http://purl.uniprot.org/uniprot/#_Q86YH1-mappedCitation-26514725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26514725 |
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| http://purl.uniprot.org/uniprot/#_P14672-mappedCitation-26514725 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26514725 |