PXD008083

PXD008083 is an original dataset announced via ProteomeXchange.

Title	Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
Description	ADP-ribosylation is a posttranslational modification that exists in monomeric and polymeric forms. Whereas the writers (e.g. ARTD1/PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well described, the enzymes involved in mono-ADP-ribosylation (MARylation) have been less well investigated. While erasers for the MARylation of glutamate/aspartate and arginine have been identified, the respective enzymes with specificity for serine are still missing. Here, we report that in vitro, ARH3 specifically binds and demodifies proteins and peptides that are MARylated. Molecular modeling and site-directed mutagenesis of ARH3 revealed that numerous residues are critical for both the mono- and the poly-ADP-ribosylhydrolase activity of ARH3. Notably, a mass spectrometry approach showed that ARH3-deficient MEFs are characterized by a specific increase in serine-ADP-ribosylation in vivo under untreated conditions as well as following hydrogen-peroxide stress. Together, our results establish ARH3 as a serine mono-ADP-ribosylhydrolase and as an important regulator of the basal and stress induced ADP-ribosylome.
HostingRepository	PRIDE
AnnounceDate	2017-12-14
AnnouncementXML	Submission_2017-12-14_04:42:37.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD008083
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Mario Leutert
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	Oxidation; Carbamidomethyl; Oxidation
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2017-10-31 02:37:13	ID requested
⏵ 1	2017-12-14 04:42:39	announced

Abplanalp J, Leutert M, Frugier E, Nowak K, Feurer R, Kato J, Kistemaker HVA, Filippov DV, Moss J, Caflisch A, Hottiger MO, Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase. Nat Commun, 8(1):2055(2017) [pubmed]

curator keyword: Biological

submitter keyword: ADP-ribosylation, PTM, HCD, EThcD, ARH3, Mono-ADP-ribosyl(-acceptor) hydrolases, PARG, PARP, Mef

Michael O. Hottiger
contact affiliation	Departement of Molecular Mechanisms of Disease, University of Zurich, Winterthurstrasse 190, 8057 Zurich, Switzerland
contact email	michael.hottiger@dmmd.uzh.ch
lab head
Mario Leutert
contact affiliation	UZH
contact email	dmmd.admin@dmmd.uzh.ch
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD008083
     1. Label: PRIDE project
     2. Name: Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase