| http://purl.uniprot.org/citations/20412061 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20412061 | http://www.w3.org/2000/01/rdf-schema#comment | "Insulin like growth factor-1 (IGF-1) is established as an anabolic factor that can induce skeletal muscle growth by activating the phosphoinositide 3-kinase/Akt/mammalian target of rapamycin (mTOR) pathway. Although this signaling pathway has been the subject of much study, the molecular mechanisms linking IGF-1 binding to mTOR activation remain poorly defined in muscle. The present study aimed to test the hypothesis that IGF-1 activation of mTOR in C2C12 myotubes requires a phosphorylation-dependent, altered distribution of the tuberous sclerosis complex (TSC)1/TSC2 complex from the membrane to the cytosol. We found that IGF-1 treatment does not affect complex formation between TSC1 and TSC2, but rather IGF-1 induces an altered distribution of the TSC1/TSC2 complex in C2C12 myotubes. In response to IGF-1 treatment, there was a relative redistribution of the TSC1/TSC2 complex, composed of TSC1 and phosphorylated TSC2, from the membrane to the cytosol. IGF-1-stimulated TSC1/TSC2 phosphorylation and redistribution were completely prevented by the phosphoinositide 3-kinase inhibitor wortmannin, but were not with the downstream mTOR inhibitor, rapamycin. When a nonphosphorylatable form of TSC2 (S939A) was overexpressed, phosphorylation-dependent binding of the scaffold protein 14-3-3 to TSC2 was diminished and no redistribution of the TSC1/TSC2 complex was observed after IGF-1 stimulation. These results indicate that TSC2 phosphorylation in response to IGF-1 treatment is necessary for the altered distribution of the TSC1/TSC2 complex to the cytosol. We suggest that this translocation is likely critical for mTOR activation by dissociating the interaction between the GTPase activating protein activity of the TSC1/TSC2 complex and its downstream target, Ras homolog enriched in brain."xsd:string |
| http://purl.uniprot.org/citations/20412061 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1742-4658.2010.07635.x"xsd:string |
| http://purl.uniprot.org/citations/20412061 | http://purl.uniprot.org/core/author | "Miyazaki M."xsd:string |
| http://purl.uniprot.org/citations/20412061 | http://purl.uniprot.org/core/author | "Esser K.A."xsd:string |
| http://purl.uniprot.org/citations/20412061 | http://purl.uniprot.org/core/author | "McCarthy J.J."xsd:string |
| http://purl.uniprot.org/citations/20412061 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20412061 | http://purl.uniprot.org/core/name | "FEBS J"xsd:string |
| http://purl.uniprot.org/citations/20412061 | http://purl.uniprot.org/core/pages | "2180-2191"xsd:string |
| http://purl.uniprot.org/citations/20412061 | http://purl.uniprot.org/core/title | "Insulin like growth factor-1-induced phosphorylation and altered distribution of tuberous sclerosis complex (TSC)1/TSC2 in C2C12 myotubes."xsd:string |
| http://purl.uniprot.org/citations/20412061 | http://purl.uniprot.org/core/volume | "277"xsd:string |
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