PXD020340

PXD020340 is an original dataset announced via ProteomeXchange.

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

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.

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]

submitter keyword: ADPr, PTM, Post-translational modification, PARP7,ADP-ribosylation

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

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PRIDE project URI

• PRIDE
  1. PXD020340
     1. Label: PRIDE project
     2. Name: Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets