Abstract
Pharmacological and Genetic Evaluation of Proposed Roles of Mitogen-activated Protein Kinase/Extracellular Signal-regulated Kinase Kinase (MEK), Extracellular Signal-regulated Kinase (ERK), and p90RSK in the Control of mTORC1 Protein Signaling by Phorbol Esters
Highlights
AUGUST 5, 2011 VOLUME 286 NUMBER 31 the control of mammalian target of rapamycin complex 1 (mTORC1) between different cell types, pointing to additional signaling connections between phorbol esters and mTORC1, which do not involve MEK/ERK
Signaling through mTORC14 regulates numerous cellular functions and is implicated in disease states such as tissue hypertrophy and cancer. mTORC1 lies downstream of numerous proto-oncogenes such as epidermal growth factor receptor, Ras, PI3K, and PKB as well as tumor suppressors including PTEN and TSC1/TSC2)
The available evidence suggests that insulin activates mTORC1 signaling through the tuberous sclerosis complex (TSC1/TSC2), which acts as a GTPase-activator protein (GAP) for the small G-protein Rheb (Ras homolog enriched in brain) [1, 13,14,15]
Summary
AUGUST 5, 2011 VOLUME 286 NUMBER 31 the control of mTORC1 between different cell types, pointing to additional signaling connections between phorbol esters and mTORC1, which do not involve MEK/ERK. These data indicate that activation of mTORC1 signaling by PMA in HEK293 cells involves MEK activity but not that of p90RSK, either through the phosphorylation of TSC2 [23, 30] or raptor [31].
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