Husain Matloob, Harrod Kevin S
Lovelace Respiratory Research Institute, Albuquerque, NM 87108, USA.
FEBS Lett. 2009 Aug 6;583(15):2517-20. doi: 10.1016/j.febslet.2009.07.005. Epub 2009 Jul 15.
Histone deacetylase 6 (HDAC6) is a multi-substrate cytoplasmic enzyme that regulates many important biological processes. Recently, some reports have implicated HDAC6 in viral infection. However, nothing is known about its regulation in virus-infected cells. The data presented here for the first time demonstrate the caspase-3-mediated cleavage of HDAC6 in influenza A virus (IAV)-infected cells. HDAC6 polypeptide contains the caspase-3 cleavage motif DMAD-S at the C-terminus, and is a caspase-3 substrate. The cleavage removes most of the C-terminal ubiquitin-binding zinc finger domain from HDAC6, which could be significant for HDAC6's role in IAV-induced apoptosis in infected cells.
组蛋白去乙酰化酶6（HDAC6）是一种多底物细胞质酶，可调节许多重要的生物学过程。最近，一些报告表明HDAC6与病毒感染有关。然而，关于其在病毒感染细胞中的调节作用尚不清楚。此处首次呈现的数据表明，在甲型流感病毒（IAV）感染的细胞中，HDAC6会被半胱天冬酶-3介导裂解。HDAC6多肽在C端含有半胱天冬酶-3裂解基序DMAD-S，是半胱天冬酶-3的底物。这种裂解从HDAC6中去除了大部分C端泛素结合锌指结构域，这可能对HDAC6在感染细胞中IAV诱导的细胞凋亡中的作用具有重要意义。
