ArticleThe Journal of biological chemistry2013
Direct inhibition of Gcn5 protein catalytic activity by polyglutamine-expanded ataxin-7.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Epigenetics in evolution and adaptation to environmental challenges: pathways for disease prevention and treatment.Epigenomics · 2025Review
- The SAGA HAT module is tethered by its SWIRM domain and modulates activity of the SAGA DUB module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Article
- Roles of Histone Acetyltransferases and Deacetylases in the Retinal Development and Diseases.Molecular neurobiology · 2023Review
- A survey of protein interactions and posttranslational modifications that influence the polyglutamine diseases.Frontiers in molecular neuroscience · 2022Review
- The Molecular Basis of Spinocerebellar Ataxia Type 7.Frontiers in neuroscience · 2022Review
- The Ada2/Ada3/Gcn5/Sgf29 histone acetyltransferase module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- Gene Deregulation and Underlying Mechanisms in Spinocerebellar Ataxias With Polyglutamine Expansion.Frontiers in neuroscience · 2020Review
- Identification and characterization of miRNAs involved in cold acclimation of zebrafish ZF4 cells.PloS one · 2020Article
- Molecular Targets and Therapeutic Strategies in Spinocerebellar Ataxia Type 7.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2019Review
- Transcriptional Dysregulation and Post-translational Modifications in Polyglutamine Diseases: From Pathogenesis to Potential Therapeutic Strategies.Frontiers in molecular neuroscience · 2018Review
- Review
- Rad51C-ATXN7 fusion gene expression in colorectal tumors.Molecular cancer · 2016Article
- Proteolytic cleavage of ataxin-7 promotes SCA7 retinal degeneration and neurological dysfunction.Human molecular genetics · 2015Article
- Poly(Q) Expansions in ATXN7 Affect Solubility but Not Activity of the SAGA Deubiquitinating Module.Molecular and cellular biology · 2015Article
- Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex.The EMBO journal · 2014Article
- The expanding role for chromatin and transcription in polyglutamine disease.Current opinion in genetics & development · 2014Review
- Pulling complexes out of complex diseases: Spinocerebellar Ataxia 7.Rare diseases (Austin, Tex.) · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Spinocerebellar ataxia type 7 (SCA7) is a neurodegenerative disease caused by polyglutamine (polyQ) expansion within the N-terminal region of the ataxin-7 protein, a known subunit of the SAGA complex. Although the mechanisms of SCA7 pathogenesis remain poorly understood, previous studies have shown perturbations in SAGA histone acetyltransferase function and transcriptional alterations. We sought to determine whether and how polyQ-expanded ataxin-7 affects SAGA catalytic activity. Here, we determined that polyQ-expanded ataxin-7 directly bound the Gcn5 catalytic core of SAGA while in association with its regulatory proteins, Ada2 and Ada3. This caused a significant decrease in Gcn5 histone acetyltransferase activity in vitro and in vivo at two SAGA-regulated galactose genes, GAL1 and GAL7. However, Gcn5 occupancy at the GAL1 and GAL7 promoters was increased in these cells, revealing a dominant-negative phenotype of the polyQ-expanded ataxin-7-incorporated, catalytically inactive SAGA. These findings suggest a dominant mechanism of polyQ-mediated SAGA inhibition that potentially contributes to SCA7 disease pathogenesis.
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