Document Detail


Mammalian TOR: a homeostatic ATP sensor.
MedLine Citation:
PMID:  11691993     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The bacterial macrolide rapamycin is an efficacious anticancer agent against solid tumors. In a hypoxic environment, the increase in mass of solid tumors is dependent on the recruitment of mitogens and nutrients. When nutrient concentrations change, particularly those of essential amino acids, the mammalian Target of Rapamycin (mTOR) functions in regulatory pathways that control ribosome biogenesis and cell growth. In bacteria, ribosome biogenesis is independently regulated by amino acids and adenosine triphosphate (ATP). Here we demonstrate that the mTOR pathway is influenced by the intracellular concentration of ATP, independent of the abundance of amino acids, and that mTOR itself is an ATP sensor.
Authors:
P B Dennis; A Jaeschke; M Saitoh; B Fowler; S C Kozma; G Thomas
Related Documents :
2085883 - Lignified materials as potential medicinal resources. iii. diversity of biological acti...
16561993 - Isolation and properties of an exocellular nuclease of serratia marcescens.
23328733 - 4-hydroxy-2(e)-nonenal (hne) catabolism and formation of hne adducts are modulated by β...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Science (New York, N.Y.)     Volume:  294     ISSN:  0036-8075     ISO Abbreviation:  Science     Publication Date:  2001 Nov 
Date Detail:
Created Date:  2001-11-05     Completed Date:  2001-12-05     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0404511     Medline TA:  Science     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1102-5     Citation Subset:  IM    
Affiliation:
The Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adaptor Proteins, Signal Transducing
Adenosine Triphosphate / metabolism*
Amino Acids / metabolism
Androstadienes / pharmacology
Carrier Proteins / metabolism
Cell Line
Deoxyglucose / pharmacology
Enzyme Activation
Homeostasis
Humans
Insulin / pharmacology
Kinetics
Phosphoproteins / metabolism
Phosphorylation
Protein Kinases / metabolism*
RNA, Transfer, Amino Acyl / metabolism
Recombinant Fusion Proteins / metabolism
Ribosomal Protein S6 Kinases / antagonists & inhibitors,  metabolism
Ribosomes / metabolism
Rotenone / pharmacology
Signal Transduction
Sirolimus / pharmacology
Chemical
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Amino Acids; 0/Androstadienes; 0/Carrier Proteins; 0/EIF4EBP1 protein, human; 0/Phosphoproteins; 0/RNA, Transfer, Amino Acyl; 0/Recombinant Fusion Proteins; 11061-68-0/Insulin; 154-17-6/Deoxyglucose; 19545-26-7/wortmannin; 53123-88-9/Sirolimus; 56-65-5/Adenosine Triphosphate; 83-79-4/Rotenone; EC 2.7.-/Protein Kinases; EC 2.7.1.-/mTOR protein; EC 2.7.11.1/Ribosomal Protein S6 Kinases

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


Previous Document:  Structural basis for recognition of the intron branch site RNA by splicing factor 1.
Next Document:  Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr.