The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation
Open accessAbstract
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 H 2 O 2 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.
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Citations
Cites
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Robin Harris, J., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,544
Physiological functions of thioredoxin and thioredoxin reductase
Arnér, E. S. J., & Holmgren, A. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01701.x · Cited by 2,525
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · cited 1×
“Inhibition of HDAC6 activity by the specific inhibitor, tubacin, or its down-regulation by siRNA, can increase accumulation of acetylated -tubulin (6, 7) and can alter cellular mobility and can increase acetylated Hsp90 (8–10), inducing client protein degradation.”
BackgroundHistone deacetylase inhibitors: molecular mechanisms of action
Xu, W. S., Parmigiani, R. B., & Marks, P. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210620 · Cited by 1,542
Self-citationThe Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,536
Marks, P. A., & Breslow, R. (2007) · Nature Biotechnology · doi:10.1038/nbt1272 · Cited by 1,196
Self-citationHistone Deacetylase Inhibitors: Overview and Perspectives
Dokmanovic, M., Clarke, C., & Marks, P. A. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-07-0324 · Cited by 1,164
Self-citationHDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153
Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0430973100 · Cited by 1,066
Hockly, E., Richon, V. M., Woodman, B., Smith, D. L., Zhou, X., Rosa, E., Sathasivam, K., Ghazi-Noori, S., Mahal, A., Lowden, P. A. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0437870100 · Cited by 845
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Cited by
Rational Design and Simple Chemistry Yield a Superior, Neuroprotective HDAC6 Inhibitor, Tubastatin A
Butler, K. V., Kalin, J., Brochier, C., Vistoli, G., Langley, B., & Kozikowski, A. P. (2010) · Journal of the American Chemical Society · doi:10.1021/ja102758v · Cited by 801
Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.283432 · Cited by 603
HDAC6 as a target for neurodegenerative diseases: what makes it different from the other HDACs?
Simões-Pires, C., Zwick, V., Nurisso, A., Schenker, E., Carrupt, P.-A., & Cuendet, M. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-7 · Cited by 341
HDAC6 is a target for protection and regeneration following injury in the nervous system
Rivieccio, M. A., Brochier, C., Willis, D. E., Walker, B. A., D'Annibale, M. A., McLaughlin, K., Siddiq, A., Kozikowski, A. P., Jaffrey, S. R., Twiss, J. L., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907935106 · Cited by 322
HDAC6 as privileged target in drug discovery: A perspective
Pulya, S., Amin, S. A., Adhikari, N., Biswas, S., Jha, T., & Ghosh, B. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2020.105274 · Cited by 253
Metadata
- Authors
- Parmigiani, R. B., Xu, W. S., Venta-Perez, G., Erdjument-Bromage, H., Yaneva, M., Tempst, P., & Marks, P. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-07-15
- Volume
- 105
- Issue
- 28
- Pages
- 9633-9638
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1519763364
- Cited by
- 321
- References
- 45
- FWCI
- 6.70
- Type
- journal article
- Language
- en
- Open access
- green
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