Acetylation of pregnane X receptor protein determines selective function independent of ligand activation

Arunima Biswas, Danielle Pasquel, Rakesh Kumar Tyagi, Sridhar Mani

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

Pregnane X receptor (PXR), like other members of its class of nuclear receptors, undergoes post-translational modification [PTM] (e.g., phosphorylation). However, it is unknown if acetylation (a major and common form of protein PTM) is observed on PXR and, if it is, whether it is of functional consequence. PXR has recently emerged as an important regulatory protein with multiple ligand-dependent functions. In the present work we show that PXR is indeed acetylated in vivo. SIRT1 (Sirtuin 1), a NAD-dependent class III histone deacetylase and a member of the sirtuin family of proteins, partially mediates deacetylation of PXR. Most importantly, the acetylation status of PXR regulates its selective function independent of ligand activation.

Original languageEnglish (US)
Pages (from-to)371-376
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume406
Issue number3
DOIs
StatePublished - Mar 18 2011

Keywords

  • Acetylation-deacetylation
  • Ligand-independent function
  • Orphan nuclear receptor
  • Pregnane X receptor
  • SIRT1 deacetylase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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