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Influenza A virus‐induced caspase‐3 cleaves the histone deacetylase 6 in infected epithelial cells
Author(s) -
Husain Matloob,
Harrod Kevin S.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.005
Subject(s) - histone deacetylase , virology , histone deacetylase 5 , chemistry , hdac11 , histone deacetylase inhibitor , virus , influenza a virus , apoptosis , histone , histone deacetylase 2 , microbiology and biotechnology , biology , biochemistry , gene
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.