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PXD008083

PXD008083 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleProteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
DescriptionADP-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.
HostingRepositoryPRIDE
AnnounceDate2017-12-14
AnnouncementXMLSubmission_2017-12-14_04:42:37.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD008083
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterMario Leutert
SpeciesList scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationListOxidation; Carbamidomethyl; Oxidation
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02017-10-31 02:37:13ID requested
12017-12-14 04:42:39announced
Publication List
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]
Keyword List
curator keyword: Biological
submitter keyword: ADP-ribosylation, PTM, HCD, EThcD, ARH3, Mono-ADP-ribosyl(-acceptor) hydrolases, PARG, PARP, Mef
Contact List
Michael O. Hottiger
contact affiliationDepartement of Molecular Mechanisms of Disease, University of Zurich, Winterthurstrasse 190, 8057 Zurich, Switzerland
contact emailmichael.hottiger@dmmd.uzh.ch
lab head
Mario Leutert
contact affiliationUZH
contact emaildmmd.admin@dmmd.uzh.ch
dataset submitter
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