Abstract
The mTOR complex-1 (mTORC1) coordinates cell growth and metabolism, acting as a restriction point under stress conditions such as low oxygen tension (hypoxia). Hypoxia suppresses mTORC1 signaling. However, the signals by which hypoxia suppresses mTORC1 are only partially understood, and a direct link between hypoxia-driven physiological stress and the regulation of mTORC1 signaling is unknown. Here we show that hypoxia results in ataxia telangiectasia mutated (ATM)-dependent phosphorylation of hypoxia-inducible factor 1-alpha (HIF-1α) on serine(696) and mediates downregulation of mTORC1 signaling. Deregulation of these pathways in pediatric solid tumor xenografts suggests a link between mTORC1 dysregulation and solid tumor development and points to an important role for hypoxic regulation of mTORC1 activity in tumor development.
Copyright © 2010 Elsevier Inc. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Animals
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Apoptosis
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Ataxia Telangiectasia Mutated Proteins
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Cell Cycle Proteins / metabolism*
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Cell Hypoxia
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DNA Damage
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DNA-Binding Proteins / metabolism*
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Enzyme Activation
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Humans
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Hypoxia-Inducible Factor 1, alpha Subunit / metabolism*
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Mechanistic Target of Rapamycin Complex 1
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Mice
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Multiprotein Complexes
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Phosphorylation
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Phosphoserine / metabolism
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Protein Serine-Threonine Kinases / metabolism*
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Proteins / metabolism*
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Signal Transduction*
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TOR Serine-Threonine Kinases
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Transcription Factors / metabolism
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Tumor Suppressor Protein p53 / metabolism
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Tumor Suppressor Proteins / metabolism*
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Xenograft Model Antitumor Assays
Substances
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Cell Cycle Proteins
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DNA-Binding Proteins
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Ddit4 protein, mouse
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Hypoxia-Inducible Factor 1, alpha Subunit
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Multiprotein Complexes
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Proteins
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Transcription Factors
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Tumor Suppressor Protein p53
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Tumor Suppressor Proteins
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Phosphoserine
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ATM protein, human
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Ataxia Telangiectasia Mutated Proteins
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Atm protein, mouse
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Mechanistic Target of Rapamycin Complex 1
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Protein Serine-Threonine Kinases
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TOR Serine-Threonine Kinases