Matthias Patrick, Yoshida Minoru, Khochbin Saadi
Friedrich Miescher Institute for Biomedical Research, Novartis Research Foundation, Basel, Switzerland.
Cell Cycle. 2008 Jan 1;7(1):7-10. doi: 10.4161/cc.7.1.5186. Epub 2007 Oct 15.
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.
自HDAC6首次被鉴定并被视为具有两个催化结构域的异常组蛋白去乙酰化酶以来,还不到十年。早期对其细胞质定位、泛素结合和微管蛋白去乙酰化酶活性的证明,使HDAC6与已知涉及其他组蛋白去乙酰化酶的一切都大相径庭。最近的发现证实了HDAC6在去乙酰化酶中具有非常独特的功能,并指出该蛋白是细胞对细胞毒性攻击反应的主要调节因子。HDAC6既表现为应激刺激的传感器,又表现为效应器,由于其广泛的活性,它介导并协调适当的细胞反应。