PMID- 23694989 OWN - NLM STAT- MEDLINE DCOM- 20140225 LR - 20240204 IS - 0219-1032 (Electronic) IS - 1016-8478 (Print) IS - 1016-8478 (Linking) VI - 35 IP - 6 DP - 2013 Jun TI - Nutrient regulation of the mTOR complex 1 signaling pathway. PG - 463-73 LID - 10.1007/s10059-013-0138-2 [doi] AB - The mammalian target of rapamycin (mTOR) is an evolutionally conserved kinase which exists in two distinct structural and functional complexes, mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). Of the two complexes, mTORC1 couples nutrient abundance to cell growth and proliferation by sensing and integrating a variety of inputs arising from amino acids, cellular stresses, energy status, and growth factors. Defects in mTORC1 regulation are implicated in the development of many metabolic diseases, including cancer and diabetes. Over the past decade, significant advances have been made in deciphering the complexity of the signaling processes contributing to mTORC1 regulation and function, but the mechanistic details are still not fully understood. In particular, how amino acid availability is sensed by cells and signals to mTORC1 remains unclear. In this review, we discuss the current understanding of nutrient-dependent control of mTORC1 signaling and will focus on the key components involved in amino acid signaling to mTORC1. FAU - Kim, Sang Gyun AU - Kim SG AD - Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. SangGyun_Kim@hms.harvard.edu FAU - Buel, Gwen R AU - Buel GR FAU - Blenis, John AU - Blenis J LA - eng GR - R01 CA046595/CA/NCI NIH HHS/United States GR - R01 GM051405/GM/NIGMS NIH HHS/United States GR - R01CA46595/CA/NCI NIH HHS/United States GR - R01GM51405/GM/NIGMS NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Research Support, Non-U.S. Gov't PT - Review DEP - 20130520 PL - United States TA - Mol Cells JT - Molecules and cells JID - 9610936 RN - 0 (Amino Acids) RN - 0 (Intercellular Signaling Peptides and Proteins) RN - 0 (Multiprotein Complexes) RN - EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1) RN - EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 2) RN - EC 2.7.11.1 (TOR Serine-Threonine Kinases) SB - IM MH - Amino Acids/*metabolism MH - Animals MH - Energy Metabolism MH - Food MH - Humans MH - Intercellular Signaling Peptides and Proteins/metabolism MH - Mechanistic Target of Rapamycin Complex 1 MH - Mechanistic Target of Rapamycin Complex 2 MH - Metabolic Diseases/immunology/*metabolism MH - Multiprotein Complexes/*metabolism MH - Nutritional Physiological Phenomena/immunology MH - *Signal Transduction MH - Stress, Physiological MH - TOR Serine-Threonine Kinases/*metabolism PMC - PMC3887879 EDAT- 2013/05/23 06:00 MHDA- 2014/02/26 06:00 PMCR- 2014/06/30 CRDT- 2013/05/23 06:00 PHST- 2013/05/03 00:00 [received] PHST- 2013/05/06 00:00 [accepted] PHST- 2013/05/23 06:00 [entrez] PHST- 2013/05/23 06:00 [pubmed] PHST- 2014/02/26 06:00 [medline] PHST- 2014/06/30 00:00 [pmc-release] AID - S1016-8478(23)05258-5 [pii] AID - molcell-35-6-463-1 [pii] AID - 10.1007/s10059-013-0138-2 [doi] PST - ppublish SO - Mol Cells. 2013 Jun;35(6):463-73. doi: 10.1007/s10059-013-0138-2. Epub 2013 May 20.