Aberrant histone acetylation, altered transcription, and retinal degeneration in a Drosophila model of polyglutamine disease are rescued by CREB-binding protein

Genes Dev. 2003 Jun 15;17(12):1463-8. doi: 10.1101/gad.1087503.

Abstract

Sequestration of the transcriptional coactivator CREB-binding protein (CBP), a histone acetyltransferase, has been implicated in the pathogenesis of polyglutamine expansion neurodegenerative disease. We used a Drosophila model to demonstrate that polyglutamine-induced neurodegeneration is accompanied by a defect in histone acetylation and a substantial alteration in the transcription profile. Furthermore, we demonstrate complete functional and morphological rescue by up-regulation of endogenous Drosophila CBP (dCBP). Rescue of the degenerative phenotype is associated with eradication of polyglutamine aggregates, recovery of histone acetylation, and normalization of the transcription profile. These findings suggest that histone acetylation is an early target of polyglutamine toxicity and indicate that transcriptional dysregulation is an important part of the pathogenesis of polyglutamine-induced neurodegeneration.

Publication types

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

MeSH terms

  • Acetylation
  • Acetyltransferases / genetics
  • Acetyltransferases / metabolism
  • Animals
  • CREB-Binding Protein
  • Cell Death / genetics
  • Disease Models, Animal
  • Gene Expression Regulation
  • Histone Acetyltransferases
  • Mutation
  • Neurons / pathology
  • Neurons / physiology
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Peptides / genetics
  • Peptides / metabolism*
  • Retinal Degeneration / genetics*
  • Retinal Degeneration / physiopathology
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Trans-Activators / genetics
  • Trans-Activators / metabolism*
  • Transcription, Genetic*

Substances

  • Nuclear Proteins
  • Peptides
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • polyglutamine
  • Acetyltransferases
  • CREB-Binding Protein
  • Histone Acetyltransferases