PXD008083 is an
original dataset announced via ProteomeXchange.
Dataset Summary
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 |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-10-31 02:37:13 | ID requested | |
⏵ 1 | 2017-12-14 04:42:39 | announced | |
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 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 | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD008083
- Label: PRIDE project
- Name: Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase