TY  - JOUR
AU  - Bütepage, Mareike
AU  - Preisinger, Christian
AU  - von Kriegsheim, Alexander
AU  - Scheufen, Anja
AU  - Lausberg, Eva
AU  - Li, Jinyu
AU  - Kappes, Ferdinand
AU  - Feederle, Regina
AU  - Ernst, Sabrina
AU  - Eckei, Laura
AU  - Krieg, Sarah
AU  - Müller-Newen, Gerhard
AU  - Rossetti, Giulia
AU  - Feijs, Karla L. H.
AU  - Verheugd, Patricia
AU  - Lüscher, Bernhard
TI  - Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
JO  - Scientific reports
VL  - 8
IS  - 1
SN  - 2045-2322
CY  - [London]
PB  - Macmillan Publishers Limited, part of Springer Nature
M1  - FZJ-2018-06522
SP  - 6748
PY  - 2018
AB  - 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 ribosomes and proteins associated with rRNA processing and ribosomal assembly factors. TARG1 localized to transcriptionally active nucleoli, which occurred independently of ADP-ribose binding. TARG1 shuttled continuously between nucleoli and nucleoplasm. In response to DNA damage, which activates ARTD1/2 (PARP1/2) and promotes synthesis of poly-ADP-ribose chains, TARG1 re-localized to the nucleoplasm. This was dependent on the ability of TARG1 to bind to poly-ADP-ribose. These findings are consistent with the observed ability of TARG1 to competitively interact with RNA and PAR chains. We propose a nucleolar role of TARG1 in ribosome assembly or quality control that is stalled when TARG1 is re-located to sites of DNA damage.
LB  - PUB:(DE-HGF)16
C6  - pmid:29712969
UR  - <Go to ISI:>//WOS:000431107100007
DO  - DOI:10.1038/s41598-018-25137-w
UR  - https://juser.fz-juelich.de/record/857531
ER  -