Influenza A virus-induced caspase-3 cleaves the histone deacetylase 6 in infected epithelial cells.
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.
Husain
Matloob
M
Lovelace Respiratory Research Institute, Albuquerque, NM 87108, USA. mhusain@lrri.org
Harrod
Kevin S
KS
D000818:Animals; D053148:Caspase 3 / Q000378:metabolism*; D002460:Cell Line; D004847:Epithelial Cells / Q000201:enzymology* / Q000821:virology*; D000073864:Histone Deacetylase 6; D006655:Histone Deacetylases / Q000378:metabolism*; D006801:Humans; D009980:Influenza A virus / Q000502:physiology*
D053148:Caspase 3; C433811:HDAC6 protein, human; D000073864:Histone Deacetylase 6; D006655:Histone Deacetylases