Autophagy substrate SQSTM1/p62 regulates chromatin ubiquitination during the DNA damage response

Autophagy. 2017 Jan 2;13(1):212-213. doi: 10.1080/15548627.2016.1245262. Epub 2016 Oct 28.

Abstract

The importance of autophagy in the DNA damage repair process is clear; however, the detailed molecular mechanism is still largely unknown. Here we found that DNA damage-induced histone H2A ubiquitination is suppressed in autophagy-deficient cells in a SQSTM1/p62 dependent manner. SQSTM1 binds and inhibits E3 ligase RNF168s activity, which is essential for H2A ubiquitination. As a result, several important factors for DNA repair cannot be recruited to the sites of DNA double-strand breaks (DSBs) in autophagy-deficient cells, leading to diminished DNA repair and increased sensitivity of cells to radiation.

Keywords: DNA damage; RNF168; autophagy; histone ubiquitination; p62.

MeSH terms

  • Autophagy
  • Cell Survival
  • Chromatin / chemistry*
  • Cytoplasm / chemistry
  • DNA Breaks, Double-Stranded
  • DNA Damage*
  • DNA Repair
  • DNA-Binding Proteins / chemistry
  • HeLa Cells
  • Histones / chemistry
  • Humans
  • Ligands
  • Plasmids
  • Sequestosome-1 Protein / chemistry*
  • Ubiquitin-Protein Ligases / chemistry*
  • Ubiquitination

Substances

  • Chromatin
  • DNA-Binding Proteins
  • Histones
  • Ligands
  • SQSTM1 protein, human
  • Sequestosome-1 Protein
  • RNF168 protein, human
  • Ubiquitin-Protein Ligases