{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wu XN"],"funding":["NIAID NIH HHS"],"pagination":["31501-11"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3173133"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["286(36)"],"pubmed_abstract":["Cell growth is influenced by environmental stress. Mammalian target of rapamycin (mTOR), the central regulator of cell growth, can be positively or negatively regulated by various stresses through different mechanisms. The p38 MAP kinase pathway is essential in cellular stress responses. Activation of MK2, a downstream kinase of p38α, enhances mTOR complex 1 (mTORC1) activity by preventing TSC2 from inhibiting mTOR activation. The p38β-PRAK cascade targets Rheb to inhibit mTORC1 activity upon glucose depletion. Here we show the activation of p38β participates in activation of mTOR complex 1 (mTORC1) induced by arsenite but not insulin, nutrients, anisomycin, or H(2)O(2). Arsenite treatment of cells activates p38β and induces interaction between p38β and Raptor, a regulatory component of mT"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Phosphorylation of Raptor by p38beta participates in arsenite-induced mammalian target of rapamycin complex 1 (mTORC1) activation."],"pmcid":["PMC3173133"],"funding_grant_id":["AI68896","R01 AI041637","R01 AI068896","AI41637"],"pubmed_authors":["Wang XK","Zheng M","Wu XN","Lu J","Zhang H","Han J","Wang YH","Zhou H","Wu SQ"],"additional_accession":[]},"is_claimable":false,"name":"Phosphorylation of Raptor by p38beta participates in arsenite-induced mammalian target of rapamycin complex 1 (mTORC1) activation.","description":"Cell growth is influenced by environmental stress. Mammalian target of rapamycin (mTOR), the central regulator of cell growth, can be positively or negatively regulated by various stresses through different mechanisms. The p38 MAP kinase pathway is essential in cellular stress responses. Activation of MK2, a downstream kinase of p38α, enhances mTOR complex 1 (mTORC1) activity by preventing TSC2 from inhibiting mTOR activation. The p38β-PRAK cascade targets Rheb to inhibit mTORC1 activity upon glucose depletion. Here we show the activation of p38β participates in activation of mTOR complex 1 (mTORC1) induced by arsenite but not insulin, nutrients, anisomycin, or H(2)O(2). Arsenite treatment of cells activates p38β and induces interaction between p38β and Raptor, a regulatory component of mT","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Sep","modification":"2025-04-18T13:22:22.601Z","creation":"2019-03-27T00:43:57Z"},"accession":"S-EPMC3173133","cross_references":{"pubmed":["21757713"],"doi":["10.1074/jbc.M111.233122","10.1074/jbc.m111.233122"]}}