Gene interactions and pathways from curated databases and text-mining

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DEPTOR — MTOR

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Peterson et al., Cell 2009 (Multiple Myeloma) : Loss of DEPTOR activates S6K1, Akt, and SGK1, promotes cell growth and survival, and activates mTORC1 and mTORC2 kinase activities ... Loss of DEPTOR activates S6K1, Akt, and SGK1, promotes cell growth and survival, and activates mTORC1 and mTORC2 kinase activities
Liu et al., J Biol Chem 2010 : Resveratrol inhibits mTOR signaling by promoting the interaction between mTOR and DEPTOR ... Taken together, our studies reveal that RSV inhibits leucine stimulated mTORC1 activation by promoting mTOR/DEPTOR interaction and thus uncover a novel mechanism by which RSV negatively regulates mTOR activity
Liu et al., Communicative & integrative biology 2011 : Resveratrol inhibits mTOR signaling by targeting DEPTOR
Zhao et al., Mol Cell 2011 : DEPTOR , an mTOR inhibitor , is a physiological substrate of SCF ( ßTrCP ) E3 ubiquitin ligase and regulates survival and autophagy ... DEPTOR , an inhibitor of mTORC1 and mTORC2 , is degraded via ubiquitin-proteasome pathway by an unknown E3 ubiquitin ligase ... DEPTOR , an inhibitor of mTORC1 and mTORC2, is degraded via ubiquitin-proteasome pathway by an unknown E3 ubiquitin ligase
Wang et al., Am J Physiol Endocrinol Metab 2012 : We and others ( Duan S et al. Mol Cell 44 : 317-324, 2011 ; Gao D et al. Mol Cell 44 : 290-303, 2011 ; Zhao Y et al. Mol Cell 44 : 304-316, 2011 ) recently reported that SCF ( ß-TrCP ) regulates cell growth and autophagy by controlling the ubiquitination and destruction of DEPTOR , an endogenous mammalian target of rapamycin inhibitor , in a phosphorylation dependent manner
Zhao et al., Neoplasia (New York, N.Y.) 2012 (Neoplasms) : Recently, we and others found that DEPTOR , a naturally occurring inhibitor of both mTORC1 and mTORC2 , was degraded by SCF ( Skp1-Cullin-F box proteins ) E3 ubiquitin ligase, the founding member of cullin-RING-ligases ( CRLs ), resulting in mTOR activation and cell proliferation ... Recently, we and others found that DEPTOR , a naturally occurring inhibitor of both mTORC1 and mTORC2, was degraded by SCF ( Skp1-Cullin-F box proteins ) E3 ubiquitin ligase, the founding member of cullin-RING-ligases ( CRLs ), resulting in mTOR activation and cell proliferation