TSC2 mediates hyperosmotic stress-induced inactivation of mTORC1
Copyright policy )TSC2 mediates hyperosmotic stress-induced inactivation of mTORC1
AbstractmTOR complex 1 (mTORC1) regulates cell growth and metabolism. mTORC1 activity is regulated via integration of positive growth-promoting stimuli and negative stress stimuli. One stress cells confront in physiological and pathophysiological contexts is hyperosmotic stress. The mechanism by which hyperosmotic stress regulates mTORC1 activity is not well understood. We show here that mild hyperosmotic stress induces a rapid and reversible inactivation of mTORC1 via a mechanism involving multiple upstream signaling pathways. We find that hyperosmotic stress causes dynamic changes in TSC2 phosphorylation by upstream kinases, such as Akt, thereby recruiting TSC2 from the cytoplasm to lysosomes where it acts on Rheb, the direct activator of mTORC1. This work puts together a signaling pathway whereby hyperosmotic stress inactivates mTORC1.
Ribosomal Protein S6 Kinases, TOR Serine-Threonine Kinases, Tumor Suppressor Proteins, Mechanistic Target of Rapamycin Complex 1, Models, Biological, Article, Cell Line, Mice, Osmotic Pressure, Stress, Physiological, Multiprotein Complexes, Tuberous Sclerosis Complex 2 Protein, Phosphoprotein Phosphatases, Animals, Humans, Marine Toxins, Lysosomes, Oxazoles, Proto-Oncogene Proteins c-akt, Monomeric GTP-Binding Proteins, Signal Transduction
Ribosomal Protein S6 Kinases, TOR Serine-Threonine Kinases, Tumor Suppressor Proteins, Mechanistic Target of Rapamycin Complex 1, Models, Biological, Article, Cell Line, Mice, Osmotic Pressure, Stress, Physiological, Multiprotein Complexes, Tuberous Sclerosis Complex 2 Protein, Phosphoprotein Phosphatases, Animals, Humans, Marine Toxins, Lysosomes, Oxazoles, Proto-Oncogene Proteins c-akt, Monomeric GTP-Binding Proteins, Signal Transduction
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