Recruitment of the protein phosphatase-1 catalytic subunit to promoters by the dual-function transcription factor RFX1

Biochem Biophys Res Commun. 2019 Feb 19;509(4):1015-1020. doi: 10.1016/j.bbrc.2019.01.011. Epub 2019 Jan 14.

Abstract

RFX proteins are a family of conserved DNA binding proteins involved in various, essential cellular and developmental processes. RFX1 is a ubiquitously expressed, dual-activity transcription factor capable of both activation and repression of target genes. The exact mechanism by which RFX1 regulates its target is not known yet. In this work, we show that the C-terminal repression domain of RFX1 interacts with the Serine/Threonine protein phosphatase PP1c, and that interaction with RFX1 can target PP1c to specific sites in the genome. Given that PP1c was shown to de-phosphorylate several transcription factors, as well as the regulatory C-terminal domain of RNA Polymerase II the recruitment of PP1c to promoters may be a mechanism by which RFX1 regulates the target genes.

Keywords: Co-repressor; PP1; Protein phosphatase; RFX1; Transcription repression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport
  • Catalytic Domain
  • Gene Expression Regulation
  • Humans
  • Phosphorylation
  • Promoter Regions, Genetic*
  • Protein Binding
  • Protein Domains
  • Protein Phosphatase 1 / metabolism*
  • Regulatory Factor X1 / metabolism*
  • Transcription Factors / metabolism

Substances

  • Regulatory Factor X1
  • Transcription Factors
  • Protein Phosphatase 1