AROS has a context‐dependent effect on SIRT1. Issue 9 (26th March 2014)

• Record Type: Journal Article
• Authors: Kokkola, Tarja; Suuronen, Tiina; Molnár, Ferdinand; Määttä, Juha; Salminen, Antero; Jarho, Elina M.; Lahtela-Kakkonen, Maija
• Is Part Of: FEBS letters. Volume 588:Issue 9(2014)
• Page Start: 1523
• Page End: 1528
• Publication Date: 2014-03-26
• Subjects: AROS -- p53 -- Protein–protein interaction -- SIRT1 -- Sirtuin; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2014.03.020
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract : AROS inhibits SIRT1 in two different in vitro enzymatic activity assays. AROS does not affect the acetylation of p53 or the activity of SIRT1 in human cells. N‐terminal deletions of SIRT1 result in loss of interaction between SIRT1 and AROS.