PXD008041-2

PXD008041 is an original dataset announced via ProteomeXchange.

Title	Proteomic characterization of the heart and skeletal muscle reveals widespread Arginine ADP-ribosylation by the ectopic ADP-ribosyltransferase ARTC1
Description	ADP-ribosylation has thus far been studied on the proteomic level mainly in cell lines and in combination with genotoxic stress. The clostridium-like ADP-ribosyltransferases (i.e. ARTC) are GPI-anchored or secreted proteins that are expressed in a highly tissue specific manner. Transcriptomic data revealed that ARTC1 is expressed in skeletal muscle and heart tissue. Although ARTC1 is highly active in vitro, identification of ARTC1 targets in vivo and subsequent characterization of ARTC1-regulated cellular processes on the proteome level has been challenging and only a few ADP-ribosylated targets are known. Using a new MS-based workflow, we provide the thus far most extensive identification of endogenous ADP-ribosylomes with hundreds of ARTC1-ADP-ribosylated proteins in C2C12 myotubes and in skeletal muscle and heart tissues from wild type and newly generated ARTC1 knockout mice. These proteins are ADP-ribosylated on arginine residues and mainly located on the cell surface or in the extracellular space. They are associated with signal transduction, transmembrane transport and muscle function. Together we provide the first comprehensive systems-level analysis of endogenous ADP-ribosylation in two different muscle tissues revealing a widespread function of ARTC1 and its targets.
HostingRepository	PRIDE
AnnounceDate	2018-08-17
AnnouncementXML	Submission_2018-08-20_03:14:52.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD008041
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; Oxidation; Carbamidomethyl
Instrument	Q Exactive HF; Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2017-10-25 05:44:48	ID requested
1	2018-08-17 01:56:28	announced
⏵ 2	2018-08-20 03:14:54	announced	Updated publication reference for PubMed record(s): 30110646.

Leutert M, Menzel S, Braren R, Rissiek B, Hopp AK, Nowak K, Bisceglie L, Gehrig P, Li H, Zolkiewska A, Koch-Nolte F, Hottiger MO, Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme. Cell Rep, 24(7):1916-1929.e5(2018) [pubmed]

curator keyword: Biological

submitter keyword: ADP-ribosylation, PTM, ARTC1, Art1, Heart, Muscle, C2C12, HCD, EThcD,

Michael O. Hottiger
contact affiliation	Department of Molecular Mechanisms of Disease, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland
contact email	michael.hottiger@dmmd.uzh.ch
lab head
Mario Leutert
contact affiliation	University of Zurich
contact email	marioleutert@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD008041
     1. Label: PRIDE project
     2. Name: Proteomic characterization of the heart and skeletal muscle reveals widespread Arginine ADP-ribosylation by the ectopic ADP-ribosyltransferase ARTC1