Leucine zipper-like domain is required for tumor suppressor ING2-mediated nucleotide excision repair and apoptosis

FEBS Lett. 2006 Jul 10;580(16):3787-93. doi: 10.1016/j.febslet.2006.05.065. Epub 2006 Jun 9.

Abstract

The plant homodomain (PHD) of ING2 was shown to regulate p53-dependent apoptosis through phosphoinositides signaling. However, the role of a predicted leucine zipper-like (LZL) motif in N-terminus of ING2 is unclear. Here, we show that LZL motif is critical for the proper functions of ING2 in DNA repair, apoptosis and chromatin remodeling after UV irradiation. Deletion of LZL domain also abrogated the association between ING2 and p53, but not between ING2 and p300, suggesting that ING2 modulates p53-dependent chromatin remodeling, apoptosis and DNA repair by functioning as a scaffold protein to mediate the interaction between p53 and p300.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Apoptosis* / radiation effects
  • Chromatin Assembly and Disassembly
  • DNA Repair*
  • DNA, Neoplasm / genetics
  • DNA, Neoplasm / metabolism
  • DNA, Neoplasm / radiation effects
  • E1A-Associated p300 Protein / metabolism
  • Histones / metabolism
  • Homeodomain Proteins / chemistry*
  • Homeodomain Proteins / genetics
  • Homeodomain Proteins / metabolism*
  • Humans
  • Leucine Zippers*
  • Protein Binding
  • Protein Structure, Tertiary
  • Receptors, Cytoplasmic and Nuclear / chemistry*
  • Receptors, Cytoplasmic and Nuclear / genetics
  • Receptors, Cytoplasmic and Nuclear / metabolism*
  • Tumor Cells, Cultured
  • Tumor Suppressor Protein p53 / metabolism
  • Tumor Suppressor Proteins / chemistry*
  • Tumor Suppressor Proteins / genetics
  • Tumor Suppressor Proteins / metabolism*
  • Ultraviolet Rays

Substances

  • DNA, Neoplasm
  • Histones
  • Homeodomain Proteins
  • ING2 protein, human
  • Receptors, Cytoplasmic and Nuclear
  • Tumor Suppressor Protein p53
  • Tumor Suppressor Proteins
  • E1A-Associated p300 Protein
  • EP300 protein, human