Polyglutamine Disease: Acetyltransferases Awry
نویسنده
چکیده
Recent evidence indicates that inhibition of histone acetyltransferases may be a primary cause of cellular pathogenesis in polyglutamine diseases such as Huntington disease; the results raise the possibility that pharmacologic manipulation of protein acetylation levels could be of therapeutic benefit.
منابع مشابه
Pcaf modulates polyglutamine pathology in a Drosophila model of Huntington's disease.
Huntingtin peptides with elongated polyglutamine domains, the root causes of Huntington's disease, hinder histone acetylation, which leads to transcriptional dysregulation. However, the range of acetyltransferases interacting with mutant Huntingtin has not been systematically evaluated. We used genetic interaction tests in Drosophila to determine whether specific acetyltransferases belonging to...
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Histone acetyltransferases have been shown to participate in many essential cellular processes, particularly those associated with activation of transcription. SAGA (Spt-Ada-Gcn5 acetyltransferase) and SLIK (SAGA-like) are two highly homologous multisubunit histone acetyltransferase complexes that were originally identified in the yeast Saccharomyces cerevisiae. Here, we identify the protein Sg...
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عنوان ژورنال:
- Current Biology
دوره 12 شماره
صفحات -
تاریخ انتشار 2002