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