HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation Journal Article

   


Authors: Parmigiani, R. B.; Xu, W. S.; Venta-Perez, G.; Erdjument-Bromage, H.; Yaneva, M.; Tempst, P.; Marks, P. A.
Article Title: HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation
Abstract: Eighteen histone deacetylases (HDACs) are present in humans, categorized into two groups: zinc-dependent enzymes (HDAC1-11) and NAD+-dependent enzymes (sirtuins 1-7). Among zinc-dependent HDACs, HDAC6 is unique. It has a cytoplasmic localization, two catalytic sites, a ubiquitin-binding site, and it selectively deacetylases α-tubulin and Hsp90. Here, we report the discovery that the redox regulatory proteins, peroxiredoxin (Prx) I and Prx II are specific targets of HDAC6. Prx are antioxidants enzymes whose main function is H2O2 reduction. Prx are elevated in many cancers and neurodegenerative diseases. The acetylated form of Prx accumulates in the absence of an active HDAC6. Acetylation of Prx increases its reducing activity, its resistance to superoxidation, and its resistance to transition to high-molecular-mass complexes. Thus, HDAC6 and Prx are targets for modulating intracellular redox status in therapeutic strategies for disorders as disparate as cancers and neurodegenerative diseases. © 2008 by The National Academy of Sciences of the USA.
Keywords: controlled study; human cell; histone deacetylase inhibitor; protein function; protein targeting; enzyme activity; cell line, tumor; histone deacetylase inhibitors; hydrogen peroxide; antioxidant; oxidative stress; peroxiredoxin; molecular weight; histone deacetylases; oxidation reduction reaction; oxidation-reduction; degenerative disease; deacetylation; acetylation; histone deacetylase 6; peroxiredoxin i; peroxiredoxin ii; peroxides; peroxiredoxins
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 105
Issue: 28
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2008-07-15
Start Page: 9633
End Page: 9638
Language: English
DOI: 10.1073/pnas.0803749105
PUBMED: 18606987
PROVIDER: scopus
PMCID: PMC2443817
DOI/URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-47749156827&partnerID=40&md5=d57beb6fa623d21077cd5041156520c4
Notes: --- - "Cited By (since 1996): 49" - "Export Date: 17 November 2011" - "CODEN: PNASA" - "Source: Scopus"
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MSK Authors
  1. Raphael B Parmigiani
    3 Parmigiani
  2. Weisheng Xu
    13 Xu
  3. Paul J Tempst
    324 Tempst
  4. Mariana M Yaneva
    9 Yaneva
  5. Gisela Venta-Perez
    23 Venta-Perez
  6. Hediye Erdjument-Bromage
    271 Erdjument-Bromage
  7. Paul Marks
    186 Marks
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