Abstract
The recent structure of a truncated mTOR in a complex with mLST8 has provided a basic framework for understanding all of the phosphoinositide 3-kinase (PI3K)-related kinases (PIKKs): mTOR, ATM, ATR, SMG-1, TRRAP and DNA-PK. The PIKK kinase domain is encircled by the FAT domain, a helical solenoid that is present in all PIKKs. PIKKs also have an extensive helical solenoid N-terminal to the FAT domain for which there is limited structural information. This N-terminal helical solenoid is essential for binding proteins that associate with the PIKKs to regulate their activity and cellular localization.
Copyright © 2014 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adaptor Proteins, Signal Transducing / chemistry
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Animals
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Ataxia Telangiectasia Mutated Proteins / chemistry
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DNA-Binding Proteins / chemistry
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Mammals
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Multiprotein Complexes / chemistry*
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Nuclear Proteins / chemistry
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Phosphatidylinositol 3-Kinases / chemistry*
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Protein Conformation
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Saccharomyces cerevisiae / chemistry
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TOR Serine-Threonine Kinases / chemistry*
Substances
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Adaptor Proteins, Signal Transducing
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DNA-Binding Proteins
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Multiprotein Complexes
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Nuclear Proteins
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transformation-transcription domain-associated protein
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Ataxia Telangiectasia Mutated Proteins
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TOR Serine-Threonine Kinases