103 Epigenomics (2015) 7(1), 103–118 ISSN 1750-1911
part of
Review
10.2217/EPI.14.69 © 2015 Future Medicine Ltd
Histone deacetylase (HDAC)6 is a member of the class IIb HDAC family. This enzyme is
zinc-dependent and mainly localized in the cytoplasm. HDAC6 is a unique isoenzyme
with two functional catalytic domains and speciic physiological roles. Indeed, HDAC6
deacetylates various substrates including α-tubulin and HSP90α, and is involved
in protein traficking and degradation, cell shape and migration. Consequently,
deregulation of HDAC6 activity was associated to a variety of diseases including cancer,
neurodegenerative diseases and pathological autoimmune response. Therefore,
HDAC6 represents an interesting potential therapeutic target. In this review, we
discuss structural features of this histone deacetylase, regulation of its expression and
activity, biological functions, implication in human disease initiation and progression.
Finally will describe novel and selective HDAC6 inhibitors.
Keywords: autoimmuneresponse•cancer•epigenetics•HDAC6•HDAC6inhibitor
•histonedeacetylase•neurodegenerativedisease
Acetylation of the ε nitrogen of lysine resi-
dues is catalyzed by histone acetyltransferases
(HATs). Deacetylation of both nuclear pro-
teins (including histones) and cytoplasmic
proteins is catalyzed by histone deacetylases
(HDACs).
In mammals, HATs are classified into two
groups according to their cellular localiza-
tion: group A is primarily nuclear, whereas
group B is essentially cytoplasmic. A clas-
sification system using their sequence simi-
larities is compromised by the lack of simi-
larity between these enzymes. However,
selected enzymes are classified according
to their sequence similarity and function
into the following families: GNAT (gen-
eral control [GC]N5 related N-acetyl-
transferase), p300/CBP (cAMP response
element-binding protein [CREB]-binding
protein), MYST (MOZ, Ybf2/Sas3, SAS2
and TIP60), TAFII250 (TBP [TATA box
binding protein]-associated factor 250
kDa) and steroid receptor cofactor (SRC)
(for review, see [1]). All HAT enzymes use
acetyl-coenzyme A as a cofactor.
There are 18 mammalian HDACs subdi-
vided into four classes based on their sequence
identity and catalytic activity (Figure 1) .
Indeed, classes I, II and IV are enzymes with
a zinc ion at the bottom of their catalytic
pocket essential for the deacetylation reac-
tion; class III enzymes do not possess this
ion, but their activity depends on the cofactor
nicotinamide adenine dinucleotide (NAD
+
).
Class I includes HDAC1, 2, 3 and 8, which
are located mainly in the nucleus due to
the presence of a nuclear localization signal
(NLS). Interestingly, HDAC3 possesses also
a nuclear export signal (NES) in the catalytic
domain. Class II is divided into two sub-
classes: subclass IIa including HDAC4, 5, 7
and 9 and subclass IIb consisting of HDAC6
and 10. Class II isoenzymes possess a NLS
as well as a NES except HDAC9 (NLS only)
and HDAC10 (NES only). Class IV corre-
sponds to HDAC11. Class III, also known as
sirtuins by analogy with yeast silent informa-
tion regulator 2 (SIR2), contains seven mem-
bers, SIRT1 to 7; some members contain
NES and/or NLS (for review, see [2]).
Histone deacetylase 6 in health and disease
Carole Seidel
1
, Michael
Schnekenburger
1
, Mario
Dicato
1
& Marc Diederich*
,2
1
LaboratoryofMolecular&Cellular
BiologyofCancer,HôpitalKirchberg,
L-2540Luxembourg,Luxembourg
2
DepartmentofPharmacy,Collegeof
Pharmacy,SeoulNationalUniversity,
Building20,Room303,1Gwanak-ro,
Gwanak-gu,Seoul151–742,Korea
*Authorforcorrespondence:
Tel.:+8228808919
marcdiederich@snu.ac.kr
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