This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Histone deacetylase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
* '''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

Retrieved from "http://52.214.119.220/wiki/index.php/Histone_deacetylase"
Personal tools