Abstract
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 specific physiological roles. Indeed, HDAC6 deacetylates various substrates including α-tubulin and HSP90α, and is involved in protein trafficking 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.
Financial & competing interests disclosure
C Seidel is recipient of a Télévie Luxembourg fellowship. M Schnekenburger is supported by a ‘Waxweiler grant for cancer prevention research’ from the Action Lions ‘Vaincre le Cancer.’ This work was supported by Télévie Luxembourg, the ‘Recherche Cancer et Sang’ foundation and ‘Recherches Scientifiques Luxembourg’ association. The authors thank ‘Een Häerz fir Kriibskrank Kanner’ association and the Action Lions ‘Vaincre le Cancer’ for generous support. M Dicato is supported by the NRF by the MEST of Korea for Tumor Microenvironment GCRC 2012-0001184 grant, by the Seoul National University (SNU) Research grant, by the Research Settlement Fund for the new faculty of SNU and by the Research Institute of Pharmaceutical Sciences. The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.