Histone deacetylase

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* '''HDAC class I''' are homologous to yeast Rpd3.<br />
* '''HDAC class I''' are homologous to yeast Rpd3.<br />
* '''HDAC class II''' are homologous to yeast HdaI.<br />
* '''HDAC class II''' are homologous to yeast HdaI.<br />
-
* '''HDAC class III''' called '''sirtuin''' - Silent Information Regulator) (SIRT) are NAD-dependent HDAC <ref>PMID:18249170</ref>.<br />
+
* '''HDAC class III''' called '''sirtuin''' - (Silent Information Regulator) (SIRT) are NAD-dependent HDAC <ref>PMID:18249170</ref>.<br />
For additional details see<br />
For additional details see<br />
* [[Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure]]<br />
* [[Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure]]<br />

Revision as of 11:33, 23 March 2016

Template:STRUCTURE 3ewf

Contents

Function

Histone deacetylase (HDAC) catalyzes the removal of acetyl group from ε-N-acetyl lysine in histones[1]. HDAC contains Zn. DNA expression is regulated by acetylation and de-acetylation. SAHA is a common inhibitor of HDAC. HDAC are classified according to their domain organization into 4 classes.

  • HDAC class I are homologous to yeast Rpd3.
  • HDAC class II are homologous to yeast HdaI.
  • HDAC class III called sirtuin - (Silent Information Regulator) (SIRT) are NAD-dependent HDAC [2].

For additional details see

Relevance

HDAC inhibitors are used in cancer therapy[3]. Sirtuins play a role in cancer, metabolic activity and neurodegenerative diseases[4].

3D Structures of histone deacetylase

Updated on 23-March-2016


References

  1. ↑ Joshi P, Greco TM, Guise AJ, Luo Y, Yu F, Nesvizhskii AI, Cristea IM. The functional interactome landscape of the human histone deacetylase family. Mol Syst Biol. 2013;9:672. doi: 10.1038/msb.2013.26. PMID:23752268 doi:http://dx.doi.org/10.1038/msb.2013.26
  2. ↑ Schwer B, Verdin E. Conserved metabolic regulatory functions of sirtuins. Cell Metab. 2008 Feb;7(2):104-12. doi: 10.1016/j.cmet.2007.11.006. PMID:18249170 doi:http://dx.doi.org/10.1016/j.cmet.2007.11.006
  3. ↑ Marks P, Rifkind RA, Richon VM, Breslow R, Miller T, Kelly WK. Histone deacetylases and cancer: causes and therapies. Nat Rev Cancer. 2001 Dec;1(3):194-202. PMID:11902574 doi:http://dx.doi.org/10.1038/35106079
  4. ↑ Yamamoto H, Schoonjans K, Auwerx J. Sirtuin functions in health and disease. Mol Endocrinol. 2007 Aug;21(8):1745-55. Epub 2007 Apr 24. PMID:17456799 doi:http://dx.doi.org/10.1210/me.2007-0079

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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