RRC ID 37911
著者 Okuda K, Ito A, Uehara T.
タイトル Regulation of Histone Deacetylase 6 Activity via S-Nitrosylation.
ジャーナル Biol Pharm Bull
Abstract Nitric oxide (NO) is a gaseous regulatory factor produced by NO synthases (NOS) and it plays several critical roles via S-nitrosylation of protein cysteine residues. Histone deacetylase (HDAC) functions in the maintenance/balance of chromatin acetylation and contributes to transcriptional supression. It has been reported that S-nitrosylation of HDAC2 is involved in the regulation of deacetylase activity. However, it remains unknown whether other subtypes of the HDAC family are S-nitrosylated. In the present study, we found that HDAC6 is a target of NO. A biotin-switch assay revealed that endogenous HDAC6 is S-nitrosylated by both NO donors and NO derived from the inducible type of NOS in cells treated with cytokines. NO led to suppressed deacetylase activity in vitro and increased acetylated α-tubulin, a major substrate for HDAC6, in A549 cells. These findings suggest that S-nitrosylation of HDAC6 plays a pivotal role in the regulation of protein acetylation.
巻・号 38(9)
ページ 1434-7
公開日 2015-1-1
DOI 10.1248/bpb.b15-00364
PMID 26328501
MeSH Acetylation Cell Line, Tumor Cysteine / analogs & derivatives Cysteine / pharmacology Histone Deacetylase 6 Histone Deacetylases / metabolism* Humans Nitric Oxide / metabolism* Nitric Oxide Donors / pharmacology Nitric Oxide Synthase Type II / metabolism S-Nitrosothiols / pharmacology
IF 1.863
引用数 14
WOS 分野 PHARMACOLOGY & PHARMACY
リソース情報
ヒト・動物細胞 A549