Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 Apr 30;8:6748. doi: 10.1038/s41598-018-25137-w

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Model of a dual function of TARG1 in both RNA- and PAR-regulated cellular processes. Under steady-state conditions, TARG1 accumulates in nucleoli but constantly shuttles between nucleoli and the nucleoplasm (1). Accumulation of TARG1 in nucleoli is mediated by direct interaction with ribosomal RNA or proteins (RP) or other nucleolar proteins (NP; 2). PARylation modulates the localization and interactome of TARG1. TARG1 re-locates to the nucleoplasm upon DNA damage-induced ARTD1/2-dependent PARylation (3). In nucleoli, TARG1 may contribute to ribosome biogenesis, e.g., by counteracting PARylation of RPs or controlling nucleolar PAR scaffolds. DNA damage-induced PARylation might serve to sequester TARG1 to the nucleoplasm to regulate PAR turnover at DNA damage sites (4). Hypothetical interactions are marked by grey arrows.