| mTOR | |||||||
|---|---|---|---|---|---|---|---|
 mTORC1 heteromer, Human | |||||||
| Identifiers | |||||||
| Symbol | MTOR | ||||||
| Alt. symbols | FRAP, FRAP2, FRAP1 | ||||||
| NCBI gene | 2475 | ||||||
| HGNC | 3942 | ||||||
| OMIM | 601231 | ||||||
| RefSeq | NM_004958 | ||||||
| UniProt | P42345 | ||||||
| Other data | |||||||
| EC number | 2.7.11.1 | ||||||
| Locus | Chr. 1 p36 | ||||||
| |||||||
| RPTOR | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | RPTOR | ||||||
| Alt. symbols | KOG1, Mip1 | ||||||
| NCBI gene | 57521 | ||||||
| HGNC | 30287 | ||||||
| OMIM | 607130 | ||||||
| RefSeq | NM_001163034.1 | ||||||
| UniProt | Q8N122 | ||||||
| Other data | |||||||
| Locus | Chr. 17 q25.3 | ||||||
| |||||||
mTORC1, also known as mammalian target of rapamycin complex 1 or mechanistic target of rapamycin complex 1, is a protein complex that functions as a nutrient/energy/redox sensor and controls protein synthesis.[1][2]
mTOR Complex 1 (mTORC1) is composed of the mTOR protein complex, regulatory-associated protein of mTOR (commonly known as raptor), mammalian lethal[clarification needed] with SEC13 protein 8 (MLST8), PRAS40 and DEPTOR.[2][3][4] This complex embodies the classic functions of mTOR, namely as a nutrient/energy/redox sensor and controller of protein synthesis.[1][2] The activity of this complex is regulated by rapamycin, insulin, growth factors, phosphatidic acid, certain amino acids and their derivatives (e.g., L-leucine and β-hydroxy β-methylbutyric acid), mechanical stimuli, and oxidative stress.[2][5][6] Recently it has been also demonstrated that cellular bicarbonate metabolism can be regulated by mTORC1 signaling.[7]
The role of mTORC1 is to activate translation of proteins.[8] In order for cells to grow and proliferate by manufacturing more proteins, the cells must ensure that they have the resources available for protein production. Thus, for protein production, and therefore mTORC1 activation, cells must have adequate energy resources, nutrient availability, oxygen abundance, and proper growth factors in order for mRNA translation to begin.[4]
- ^ a b Hay N, Sonenberg N (August 2004). "Upstream and downstream of mTOR". Genes & Development. 18 (16): 1926–1945. doi:10.1101/gad.1212704. PMID 15314020.
- ^ a b c d Kim DH, Sarbassov DD, Ali SM, et al. (July 2002). "mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery". Cell. 110 (2): 163–175. doi:10.1016/S0092-8674(02)00808-5. PMID 12150925. S2CID 4656930.
- ^ Kim DH, Sarbassov DD, Ali SM, et al. (April 2003). "GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR". Molecular Cell. 11 (4): 895–904. doi:10.1016/S1097-2765(03)00114-X. PMID 12718876.
- ^ a b Wullschleger S, Loewith R, Hall MN (February 2006). "TOR signaling in growth and metabolism". Cell. 124 (3): 471–484. doi:10.1016/j.cell.2006.01.016. PMID 16469695. S2CID 17195001.
- ^ Fang Y, Vilella-Bach M, Bachmann R, et al. (November 2001). "Phosphatidic acid-mediated mitogenic activation of mTOR signaling". Science. 294 (5548): 1942–1945. Bibcode:2001Sci...294.1942F. doi:10.1126/science.1066015. PMID 11729323. S2CID 44444716.
- ^ Bond P (March 2016). "Regulation of mTORC1 by growth factors, energy status, amino acids and mechanical stimuli at a glance". Journal of the International Society of Sports Nutrition. 13: 8. doi:10.1186/s12970-016-0118-y. PMC 4774173. PMID 26937223.
- ^ Ali E, Liponska A, O'Hara B, et al. (June 2022). "The mTORC1-SLC4A7 axis stimulates bicarbonate import to enhance de novo nucleotide synthesis". Molecular Cell. 82 (1): 3284–3298.e7. doi:10.1016/j.molcel.2022.06.008. PMC 9444906. PMID 35772404.
- ^ Sharma A, Hoeffer CA, Takayasu Y, et al. (January 2010). "Dysregulation of mTOR signaling in fragile X syndrome". The Journal of Neuroscience. 30 (2): 694–702. doi:10.1523/JNEUROSCI.3696-09.2010. PMC 3665010. PMID 20071534.