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The adaptor protein p66Shc inhibits mTOR-dependent anabolic metabolism.
- Source :
-
Science signaling [Sci Signal] 2014 Feb 18; Vol. 7 (313), pp. ra17. Date of Electronic Publication: 2014 Feb 18. - Publication Year :
- 2014
-
Abstract
- Adaptor proteins link surface receptors to intracellular signaling pathways and potentially control the way cells respond to nutrient availability. Mice deficient in p66Shc, the most recently evolved isoform of the Shc1 adaptor proteins and a mediator of receptor tyrosine kinase signaling, display resistance to diabetes and obesity. Using quantitative mass spectrometry, we found that p66Shc inhibited glucose metabolism. Depletion of p66Shc enhanced glycolysis and increased the allocation of glucose-derived carbon into anabolic metabolism, characteristics of a metabolic shift called the Warburg effect. This change in metabolism was mediated by the mammalian target of rapamycin (mTOR) because inhibition of mTOR with rapamycin reversed the glycolytic phenotype caused by p66Shc deficiency. Thus, unlike the other isoforms of Shc1, p66Shc appears to antagonize insulin and mTOR signaling, which limits glucose uptake and metabolism. Our results identify a critical inhibitory role for p66Shc in anabolic metabolism.
- Subjects :
- Animals
Antibiotics, Antineoplastic pharmacology
Glucose genetics
Glucose metabolism
Glycolysis drug effects
HeLa Cells
Humans
Mice
Mice, Knockout
Shc Signaling Adaptor Proteins genetics
Signal Transduction drug effects
Sirolimus pharmacology
Src Homology 2 Domain-Containing, Transforming Protein 1
TOR Serine-Threonine Kinases antagonists & inhibitors
TOR Serine-Threonine Kinases genetics
Glycolysis physiology
Shc Signaling Adaptor Proteins metabolism
Signal Transduction physiology
TOR Serine-Threonine Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1937-9145
- Volume :
- 7
- Issue :
- 313
- Database :
- MEDLINE
- Journal :
- Science signaling
- Publication Type :
- Academic Journal
- Accession number :
- 24550542
- Full Text :
- https://doi.org/10.1126/scisignal.2004785