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Infection Reveals a Modification of SIRT2 Critical for Chromatin Association.

Abstract：

:Sirtuin 2 is a nicotinamide-adenine-dinucleotide-dependent deacetylase that regulates cell processes such as carcinogenesis, cell cycle, DNA damage, and infection. Subcellular localization of SIRT2 is crucial for its function but is poorly understood. Infection with the bacterial pathogen Listeria monocytogenes, which relocalizes SIRT2 from the cytoplasm to the chromatin, provides an ideal stimulus for the molecular study of this process. In this report, we provide a map of SIRT2 post-translational modification sites and focus on serine 25 phosphorylation. We show that infection specifically induces dephosphorylation of S25, an event essential for SIRT2 chromatin association. Furthermore, we identify a nuclear complex formed by the phosphatases PPM1A and PPM1B, with SIRT2 essential for controlling H3K18 deacetylation and SIRT2-mediated gene repression during infection and necessary for a productive Listeria infection. This study reveals a molecular mechanism regulating SIRT2 function and localization, paving the way for understanding other SIRT2-regulated cellular processes.

journal_name

Cell Rep

journal_title

Cell reports

authors

Pereira JM,Chevalier C,Chaze T,Gianetto Q,Impens F,Matondo M,Cossart P,Hamon MA

doi

10.1016/j.celrep.2018.03.116

subject

Has Abstract

pub_date

2018-04-24 00:00:00

pages

1124-1137

issue

4

issn

2211-1247

pii

S2211-1247(18)30492-3

journal_volume

23

pub_type

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