Class IIa HDACs – new insights into their functions in physiology and pathology
HDAC4, 5, 7 and 9 constitute the class IIa histone deacetylases (HDACs) within the large family of protein deacetylases. Class IIa HDACs have unique features that distinguish them from other HDACs. They contain an N‐terminal domain that is required for their interaction with tissue‐specific transcri...
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Published in | The FEBS journal Vol. 282; no. 9; pp. 1736 - 1744 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
England
Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
01.05.2015
Blackwell Publishing Ltd |
Subjects | |
Online Access | Get full text |
ISSN | 1742-464X 1742-4658 1742-4658 |
DOI | 10.1111/febs.13061 |
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Summary: | HDAC4, 5, 7 and 9 constitute the class IIa histone deacetylases (HDACs) within the large family of protein deacetylases. Class IIa HDACs have unique features that distinguish them from other HDACs. They contain an N‐terminal domain that is required for their interaction with tissue‐specific transcription factors and recruitment to their target genes. The N‐terminal domain on class IIa HDACs also bears conserved serine residues that undergo signal‐dependent phosphorylation, which brings about nuclear export of the enzymes and de‐repression of their targets. One of the most important aspects of class IIa HDACs is their expression in specific tissues and organs within the organism, where they have crucial roles in development and differentiation processes. This review brings up to date our knowledge of the physiological and pathological functions of class IIa HDACs, focusing in particular on the most recent discoveries from in vivo studies of mouse model systems. |
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Bibliography: | http://dx.doi.org/10.1111/febs.13061 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 ObjectType-Review-3 content type line 23 |
ISSN: | 1742-464X 1742-4658 1742-4658 |
DOI: | 10.1111/febs.13061 |