Proteomics

Dataset Information

0

Nucleolar-nucleoplasmic shuttling of the RNA-binding macrodomain-containing TARG1 is controlled by DNA damage-induced poly-ADP-ribose and implies functions in ribosome biogenesis

ABSTRACT: In this project we employed affinity purification mass spectrometry to determine the interactome of the macrodomain containing protein TARG1/OARD1. TARG1 functions as a hydrolase towards mono-ADP-ribosylation (MARylation). TARG1 sowed strong binding to ribosomes and proteins associated with rRNA processing. However, when poly-ADP- ribosylation (PARylation) was present in the cellular lysate, TARG1 was found to interacts with DNA repair and chromatin-associated proteins, including ARTD1, in a PARylation-dependent manner. PARylation events also lead to a change in the subcellular localization of TARG1, which was found to reside in the nucleolus in resting cells, and shuttle to the nucleoplasm upon PARylation

INSTRUMENT(S): LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Fibroblast

DISEASE(S): Mixed Disorder As Reaction To Stress

SUBMITTER: Christian Preisinger  

LAB HEAD: Dr Christian Preisinger

PROVIDER: PXD008748 | Pride | 2018-04-23

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
140930_BT_AMAYA_010814_TARG-CAM.raw Raw
140930_BT_AMAYA_010814_TARG-CAM_141005201114.raw Raw
140930_BT_AMAYA_2309_CAM-TAP.raw Raw
140930_BT_AMAYA_2309_CAM-TAP_141005151753.raw Raw
140930_BT_AMAYA_2309_CAM-TARG.raw Raw
Items per page:
1 - 5 of 23
altmetric image

Publications

Macrodomains are conserved protein folds associated with ADP-ribose binding and turnover. ADP-ribosylation is a posttranslational modification catalyzed primarily by ARTD (aka PARP) enzymes in cells. ARTDs transfer either single or multiple ADP-ribose units to substrates, resulting in mono- or poly-ADP-ribosylation. TARG1/C6orf130 is a macrodomain protein that hydrolyzes mono-ADP-ribosylation and interacts with poly-ADP-ribose chains. Interactome analyses revealed that TARG1 binds strongly to ri  ...[more]

Similar Datasets

Proteomics PARP14 is a PARP with both ADP-ribosyl transferase 1 and hydrolase activities
2023-08-14 | PXD043452 | Pride
Proteomics Systems-wide analysis of serine-ADP-ribosylation reveals widespread occurrence and site-specific overlap with phosphorylation (part 2, phosphorylation data)
2018-08-29 | PXD009931 | Pride
Proteomics Tankyrase-mediated ADP-ribosylation is a novel regulator of TNF-induced death
2022-06-09 | PXD032131 | Pride
Proteomics Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
2017-12-14 | PXD008083 | Pride
Proteomics ATM INDUCES MACROD2 NUCLEAR EXPORT UPON DNA DAMAGE
2016-10-12 | PXD003712 | Pride
Proteomics Integrative functional proteomics identifies PARP1 protein complex differences and PARP inhibitor-mediated DDR and AKT-mTOR signaling in ovarian carcinoma: Chemical Proteomics
2022-10-21 | PXD029424 | Pride
Proteomics Oxidative stress induced ADP-ribosylome
2016-11-13 | MSV000080334 | MassIVE
Proteomics A chromatin re-localization screen for the identification of Poly-ADP-ribosylation (PARylation)-dependent DNA repair factors.
2024-01-26 | PXD045229 | Pride
Genomics Genome-wide analysis of ADP-ribosylation by ADPr-ChAP reveals its association with chromatin after oxidative stress
2016-02-04 | GSE69885 | GEO
Transcriptomics Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease
2021-05-20 | GSE167060 | GEO