Regulation of mTORC1 by amino acids
The mechanistic target of rapamycin complex I (mTORC1) is a central regulator of cellular and organismal growth, and hyperactivation of this pathway is implicated in the pathogenesis of many human diseases including cancer and diabetes. mTORC1 promotes growth in response to the availability of nutri...
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Elsevier
2017
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Online Access: | http://hdl.handle.net/1721.1/110392 https://orcid.org/0000-0002-1446-7256 |
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author | Bar-Peled, Liron Sabatini, David |
author2 | Massachusetts Institute of Technology. Department of Biology |
author_facet | Massachusetts Institute of Technology. Department of Biology Bar-Peled, Liron Sabatini, David |
author_sort | Bar-Peled, Liron |
collection | MIT |
description | The mechanistic target of rapamycin complex I (mTORC1) is a central regulator of cellular and organismal growth, and hyperactivation of this pathway is implicated in the pathogenesis of many human diseases including cancer and diabetes. mTORC1 promotes growth in response to the availability of nutrients, such as amino acids, which drive mTORC1 to the lysosomal surface, its site of activation. How amino acid levels are communicated to mTORC1 is only recently coming to light by the discovery of a lysosome-based signaling system composed of Rags (Ras-related GTPases) and Ragulator v-ATPase, GATOR (GAP activity towards Rags), and folliculin (FLCN) complexes. Increased understanding of this pathway will not only provide insight into growth control but also into the human pathologies triggered by its deregulation. |
first_indexed | 2024-09-23T10:30:23Z |
format | Article |
id | mit-1721.1/110392 |
institution | Massachusetts Institute of Technology |
language | en_US |
last_indexed | 2024-09-23T10:30:23Z |
publishDate | 2017 |
publisher | Elsevier |
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spelling | mit-1721.1/1103922022-09-30T21:31:24Z Regulation of mTORC1 by amino acids Bar-Peled, Liron Sabatini, David Massachusetts Institute of Technology. Department of Biology Koch Institute for Integrative Cancer Research at MIT Bar-Peled, Liron Sabatini, David The mechanistic target of rapamycin complex I (mTORC1) is a central regulator of cellular and organismal growth, and hyperactivation of this pathway is implicated in the pathogenesis of many human diseases including cancer and diabetes. mTORC1 promotes growth in response to the availability of nutrients, such as amino acids, which drive mTORC1 to the lysosomal surface, its site of activation. How amino acid levels are communicated to mTORC1 is only recently coming to light by the discovery of a lysosome-based signaling system composed of Rags (Ras-related GTPases) and Ragulator v-ATPase, GATOR (GAP activity towards Rags), and folliculin (FLCN) complexes. Increased understanding of this pathway will not only provide insight into growth control but also into the human pathologies triggered by its deregulation. National Institutes of Health (U.S.) (CA103866) National Institutes of Health (U.S.) (AI473890 United States. Department of Defense (W81XWH-07-0448) 2017-06-30T17:59:37Z 2017-06-30T17:59:37Z 2014-07 Article http://purl.org/eprint/type/JournalArticle 0962-8924 http://hdl.handle.net/1721.1/110392 Bar-Peled, Liron, and David M. Sabatini. “Regulation of mTORC1 by Amino Acids.” Trends in Cell Biology 24, no. 7 (July 2014): 400–406. https://orcid.org/0000-0002-1446-7256 en_US http://dx.doi.org/10.1016/j.tcb.2014.03.003 Trends in Cell Biology Creative Commons Attribution-NonCommercial-NoDerivs License http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf Elsevier PMC |
spellingShingle | Bar-Peled, Liron Sabatini, David Regulation of mTORC1 by amino acids |
title | Regulation of mTORC1 by amino acids |
title_full | Regulation of mTORC1 by amino acids |
title_fullStr | Regulation of mTORC1 by amino acids |
title_full_unstemmed | Regulation of mTORC1 by amino acids |
title_short | Regulation of mTORC1 by amino acids |
title_sort | regulation of mtorc1 by amino acids |
url | http://hdl.handle.net/1721.1/110392 https://orcid.org/0000-0002-1446-7256 |
work_keys_str_mv | AT barpeledliron regulationofmtorc1byaminoacids AT sabatinidavid regulationofmtorc1byaminoacids |