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Class II a HDAC s – new insights into their functions in physiology and pathology
Author(s) -
Parra Maribel
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13061
Subject(s) - class (philosophy) , chemistry , biology , microbiology and biotechnology , computer science , artificial intelligence
HDAC 4, 5, 7 and 9 constitute the class II a histone deacetylases ( HDAC s) within the large family of protein deacetylases. Class II a HDAC s have unique features that distinguish them from other HDAC s. 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 II a HDAC s 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 II a HDAC s 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 II a HDAC s, focusing in particular on the most recent discoveries from in vivo studies of mouse model systems.