PIKKs--the solenoid nest where partners and kinases meet

Curr Opin Struct Biol. 2014 Dec:29:134-42. doi: 10.1016/j.sbi.2014.11.003. Epub 2014 Dec 3.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry
  • Animals
  • Ataxia Telangiectasia Mutated Proteins / chemistry
  • DNA-Binding Proteins / chemistry
  • Mammals
  • Multiprotein Complexes / chemistry*
  • Nuclear Proteins / chemistry
  • Phosphatidylinositol 3-Kinases / chemistry*
  • Protein Conformation
  • Saccharomyces cerevisiae / chemistry
  • TOR Serine-Threonine Kinases / chemistry*

Substances

  • Adaptor Proteins, Signal Transducing
  • DNA-Binding Proteins
  • Multiprotein Complexes
  • Nuclear Proteins
  • transformation-transcription domain-associated protein
  • Ataxia Telangiectasia Mutated Proteins
  • TOR Serine-Threonine Kinases