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MTOR  Protein, Antibody, ELISA Kit, cDNA Clone

MTOR Related Area

MTOR Related Protein, Antibody, cDNA Gene, and ELISA Kits

MTOR Related Protein, Antibody, cDNA Gene, and ELISA Kits

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MTOR Summary & Protein Information

MTOR Background

Catalytic activity: ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation: ENZYME REGULATION: Activation of mTORC1 by growth factors such as insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase a potent activator of the protein kinase activity of mTORC1. Insulin-stimulated and amino acid-dependent phosphorylation at Ser-1261 promotes autophosphorylation and the activation of mTORC1. Activation by amino acids requires relocalization of the mTORC1 complex to lysosomes that is mediated by the Ragulator complex, SLC38A9, and the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD (PubMed:18497260, PubMed:20381137, PubMed:25561175, PubMed:25567906). On the other hand, low cellular energy levels can inhibit mTORC1 through activation of PRKAA1 while hypoxia inhibits mTORC1 through a REDD1-dependent mechanism which may also require PRKAA1. The kinase activity of MTOR within the mTORC1 complex is positively regulated by MLST8 and negatively regulated by DEPTOR and AKT1S1. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. MTOR is the target of the immunosuppressive and anti-cancer drug rapamycin which acts in complex with FKBP1A/FKBP12, and specifically inhibits its kinase activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. It may be regulated by RHEB but in an indirect manner through the PI3K signaling pathway. {ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15545625, ECO:0000269|PubMed:17386266, ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906}.
Subunit structure: Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. The mTORC1 complex is a 1 Md obligate dimer of two stoichiometric heterotetramers with overall dimensions of 290 A x 210 A x 135 A. It has a rhomboid shape and a central cavity, the dimeric interfaces are formed by interlocking interactions between the two MTOR and the two RPTOR subunits. the MLST8 subunits forms distal foot-like protuberances, and contacts only one MTOR within the complex, while the small PRAS40 localizes to the midsection of the central core, in close proximity to RPTOR. Part of the mammalian target of rapamycin COmplex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts with PPAPDC3 and PML. Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex. Interacts with UBQLN1. Interacts with TTI1 and TELO2. Interacts with CLIP1; phosphorylates and regulates CLIP1. Interacts with NBN. Interacts with HTR6 (PubMed:23027611). {ECO:0000269|PubMed:10089303, ECO:0000269|PubMed:11853878, ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926, ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:17386266, ECO:0000269|PubMed:17599906, ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:20427287, ECO:0000269|PubMed:20542007, ECO:0000269|PubMed:20801936, ECO:0000269|PubMed:20810650, ECO:0000269|PubMed:23027611, ECO:0000269|PubMed:23636326, ECO:0000269|PubMed:23762398, ECO:0000269|PubMed:8662507}.
Domain: The kinase domain (PI3K/PI4K) is intrinsically active but has a highly restricted catalytic center. {ECO:0000269|PubMed:23636326}.; The FAT domain forms three discontinuous subdomains of alpha-helical TPR repeats plus a single subdomain of HEAT repeats. The four domains pack sequentially to form a C-shaped a-solenoid that clamps onto the kinase domain (PubMed:23636326). {ECO:0000269|PubMed:23636326}.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Lysosome. Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Shuttles between cytoplasm and nucleus. Accumulates in the nucleus in response to hypoxia (By similarity). Targeting to lysosomes depends on amino acid availability and RRAGA and RRAGB. {ECO:0000250}.
Tissue specificity: Expressed in numerous tissues, with highest levels in testis. {ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:7809080}.
Post-translational: Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation. Phosphorylation in the kinase domain modulates the interactions of MTOR with RPTOR and PRAS40 and leads to increased intrinsic mTORC1 kinase activity. Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity. {ECO:0000269|PubMed:15905173, ECO:0000269|PubMed:18669648, ECO:0000269|PubMed:18691976, ECO:0000269|PubMed:19145465, ECO:0000269|PubMed:19369195, ECO:0000269|PubMed:19487463, ECO:0000269|PubMed:20068231, ECO:0000269|PubMed:21576368, ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:23429704, ECO:0000269|PubMed:24247430}.
Sequence similarity: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.; Contains 1 FAT domain. {ECO:0000255|PROSITE-ProRule:PRU00534}.; Contains 1 FATC domain. {ECO:0000255|PROSITE-ProRule:PRU00535}.; Contains 32 HEAT repeats. {ECO:0000305}.; Contains 1 PI3K/PI4K domain. {ECO:0000255|PROSITE-ProRule:PRU00269}.; Contains 16 TPR repeats. {ECO:0000305}.
General information above from UniProt

MTOR Alternative Name

MTOR Related Studies