HDAC6 a new cellular stress surveillance factor

Less than a decade has passed since HDAC6 was first identified and regarded as an unusual histone deacetylase harbouring two catalytic domains. Early demonstration of its cytoplasmic localisation, its ubiquitin-binding and its tubulin-deacetylase activities took HDAC6 far away from everything known...

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Published inCell cycle (Georgetown, Tex.) Vol. 7; no. 1; pp. 7 - 10
Main Authors Matthias, Patrick, Yoshida, Minoru, Khochbin, Saadi
Format Journal Article
LanguageEnglish
Published United States Taylor & Francis 01.01.2008
Subjects
Acetylation
Animals
Apoptosis - genetics
Apoptosis - physiology
Autophagy - genetics
Autophagy - physiology
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cell Cycle - genetics
Cell Cycle - physiology
Cycle
Cytoskeleton - enzymology
Cytoskeleton - genetics
Cytoskeleton - physiology
Histone Deacetylase 6
Histone Deacetylases - chemistry
Histone Deacetylases - metabolism
Histone Deacetylases - physiology
Humans
Landes
Mice
Organogenesis
Oxidative Stress - genetics
Oxidative Stress - physiology
Proteins
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Summary:Less than a decade has passed since HDAC6 was first identified and regarded as an unusual histone deacetylase harbouring two catalytic domains. Early demonstration of its cytoplasmic localisation, its ubiquitin-binding and its tubulin-deacetylase activities took HDAC6 far away from everything known to involve other histone-deacetylases. Recent discoveries confirmed the very unique functions of HDAC6 among deacetylases and pointed to this protein as a master regulator of cell response to cytotoxic assaults. HDAC6 appears both as a sensor of stressful stimuli and as an effector, which, thanks to its wide range of activities, mediates and coordinates appropriate cell responses.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:1538-4101
1551-4005
DOI:10.4161/cc.7.1.5186