Document Detail

Amino acids and mTORC1: from lysosomes to disease.
MedLine Citation:
PMID:  22749019     Owner:  NLM     Status:  MEDLINE    
The mechanistic target of rapamycin (mTOR) kinase controls growth and metabolism, and its deregulation underlies the pathogenesis of many diseases, including cancer, neurodegeneration, and diabetes. mTOR complex 1 (mTORC1) integrates signals arising from nutrients, energy, and growth factors, but how exactly these signals are propagated await to be fully understood. Recent findings have placed the lysosome, a key mediator of cellular catabolism, at the core of mTORC1 regulation by amino acids. A multiprotein complex that includes the Rag GTPases, Ragulator, and the v-ATPase forms an amino acid-sensing machinery on the lysosomal surface that affects the decision between cell growth and catabolism at multiple levels. The involvement of a catabolic organelle in growth signaling may have important implications for our understanding of mTORC1-related pathologies.
Alejo Efeyan; Roberto Zoncu; David M Sabatini
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review     Date:  2012-06-28
Journal Detail:
Title:  Trends in molecular medicine     Volume:  18     ISSN:  1471-499X     ISO Abbreviation:  Trends Mol Med     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-09-03     Completed Date:  2013-01-16     Revised Date:  2013-09-30    
Medline Journal Info:
Nlm Unique ID:  100966035     Medline TA:  Trends Mol Med     Country:  England    
Other Details:
Languages:  eng     Pagination:  524-33     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Ltd. All rights reserved.
Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.
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MeSH Terms
Amino Acids / metabolism*
Diabetes Mellitus / metabolism
Lysosomes / metabolism*
Multiprotein Complexes / genetics,  metabolism*
Neoplasms / metabolism
Neurodegenerative Diseases / metabolism
TOR Serine-Threonine Kinases / genetics,  metabolism*
Grant Support
R01 CA103866/CA/NCI NIH HHS; R01 CA103866/CA/NCI NIH HHS; R01 CA129105/CA/NCI NIH HHS; R01 CA129105/CA/NCI NIH HHS; R37 AI047389/AI/NIAID NIH HHS; R37 AI047389/AI/NIAID NIH HHS; //Howard Hughes Medical Institute
Reg. No./Substance:
0/Amino Acids; 0/Multiprotein Complexes; 0/mechanistic target of rapamycin complex 1; EC Serine-Threonine Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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