CHIPping away at base excision repair

Mol Cell. 2008 Feb 29;29(4):413-5. doi: 10.1016/j.molcel.2008.02.004.

Abstract

In this issue of Molecular Cell, Parsons et al. (2008) report that the E3 ubiquitin ligase CHIP regulates the stability of the base excision repair (BER) proteins XRCC1 and DNA Pol beta, adding a new level of regulation for BER.

Publication types

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

MeSH terms

  • Animals
  • DNA Damage
  • DNA Polymerase beta / genetics
  • DNA Polymerase beta / metabolism
  • DNA Repair*
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Humans
  • Macromolecular Substances / metabolism
  • Protein Processing, Post-Translational
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism*
  • X-ray Repair Cross Complementing Protein 1

Substances

  • DNA-Binding Proteins
  • Macromolecular Substances
  • X-ray Repair Cross Complementing Protein 1
  • XRCC1 protein, human
  • STUB1 protein, human
  • Ubiquitin-Protein Ligases
  • DNA Polymerase beta