AROS has a context-dependent effect on SIRT1

FEBS Lett. 2014 May 2;588(9):1523-8. doi: 10.1016/j.febslet.2014.03.020. Epub 2014 Mar 26.

Abstract

The modulation of protein deacetylase SIRT1 has a vast therapeutic potential in treatment of several aging-associated diseases. Active regulator of SIRT1 (AROS) is a small endogenous protein which was originally reported to activate SIRT1 through a direct interaction in cancer cells. We show that the interaction between the two proteins is weak and does not alter the activity of SIRT1 in non-cancerous human cells. The results of different in vitro SIRT1 activity assays disclosed AROS as an inhibitor of SIRT1. The functional relationship between AROS and SIRT1 proved to be dependent on the biological context and experimental setting.

Keywords: AROS; Protein–protein interaction; SIRT1; Sirtuin; p53.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Epithelial Cells / enzymology
  • HEK293 Cells
  • Histones / chemistry
  • Humans
  • NAD / chemistry
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism*
  • Protein Binding
  • Protein Processing, Post-Translational
  • Retinal Pigment Epithelium / cytology
  • Sirtuin 1 / chemistry
  • Sirtuin 1 / metabolism*
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Histones
  • Nuclear Proteins
  • RPS19BP1 protein, human
  • TP53 protein, human
  • Transcription Factors
  • Tumor Suppressor Protein p53
  • NAD
  • SIRT1 protein, human
  • Sirtuin 1