PXD020340 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets |
Description | Poly(ADP-ribose) polymerase 7 (PARP7) has emerged as a critically important member of a large enzyme family that catalyze mono-ADP-ribosylation (MARylation) in mammalian cells. Unlike other PARPs, PARP7 is expressed in many different cell types and is upregulated by diverse stimuli, such as toxins, growth factors, steroid hormones, and immunomodulatory ligands. Recent evidence by several independent studies show that PARP7 is a critical regulator of the innate immune response. What remains unclear is the mechanism by which PARP7 regulates this process as well as other cellular processes. This is because the protein targets, and the specific amino acid sites, of PARP7 MARylation are largely unknown. Here, we combine chemical genetics, proximity labeling, and proteome-wide amino acid ADP-ribosylation (ADPr) site profiling for identifying the direct targets and sites of PARP7-mediated MARylation. We found that the inactive PARP family member, PARP13—a critical regulator of the innate antiviral immune response—is a major target of PARP7, and is preferentially MARylated on cysteine residues in its RNA binding zinc finger domain. Proteome-wide MARylation analysis reveals cysteine as a major ADPr acceptor of PARP7. These studies not only provide insight into PARP7 targeting and MARylation site preference, but also serve as an important resource for further understanding PARP7 function in the innate immune response and other pathways. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_05:30:09.634.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Sara Larsen |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | adenosine diphosphoribosyl (ADP-ribosyl) modified residue |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-07-13 17:22:41 | ID requested | |
1 | 2021-11-04 00:21:14 | announced | |
⏵ 2 | 2024-10-22 05:30:10 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.7554/elife.60480; |
Rodriguez KM, Buch-Larsen SC, Kirby IT, Siordia IR, Hutin D, Rasmussen M, Grant DM, David LL, Matthews J, Nielsen ML, Cohen MS, Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets. Elife, 10():(2021) [pubmed] |
Keyword List
submitter keyword: ADPr, PTM, Post-translational modification, PARP7,ADP-ribosylation |
Contact List
Michael Lund Nielsen |
contact affiliation | Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark |
contact email | michael.lund.nielsen@cpr.ku.dk |
lab head | |
Sara Larsen |
contact affiliation | NNF Center for Protein Research |
contact email | sara.larsen@cpr.ku.dk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD020340
- Label: PRIDE project
- Name: Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets