Regulation of Histone Deacetylase 6 Activity <i>via</i> <i>S</i>-Nitrosylation

Access this Article

Author(s)

Abstract

Nitric oxide (NO) is a gaseous regulatory factor produced by NO synthases (NOS) and it plays several critical roles <i>via</i> <i>S</i>-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 <i>S</i>-nitrosylation of HDAC2 is involved in the regulation of deacetylase activity. However, it remains unknown whether other subtypes of the HDAC family are <i>S</i>-nitrosylated. In the present study, we found that HDAC6 is a target of NO. A biotin-switch assay revealed that endogenous HDAC6 is <i>S</i>-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 <i>in vitro</i> and increased acetylated α-tubulin, a major substrate for HDAC6, in A549 cells. These findings suggest that <i>S</i>-nitrosylation of HDAC6 plays a pivotal role in the regulation of protein acetylation.

Journal

  • Biological and Pharmaceutical Bulletin

    Biological and Pharmaceutical Bulletin 38(9), 1434-1437, 2015

    The Pharmaceutical Society of Japan

Codes

  • NII Article ID (NAID)
    130005096977
  • NII NACSIS-CAT ID (NCID)
    AA10885497
  • Text Lang
    ENG
  • ISSN
    0918-6158
  • NDL Article ID
    026699494
  • NDL Call No.
    Z53-V41
  • Data Source
    NDL  J-STAGE 
Page Top