Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription

Abstract 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-...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Mareike Bütepage, Christian Preisinger, Alexander von Kriegsheim, Anja Scheufen, Eva Lausberg, Jinyu Li, Ferdinand Kappes, Regina Feederle, Sabrina Ernst, Laura Eckei, Sarah Krieg, Gerhard Müller-Newen, Giulia Rossetti, Karla L. H. Feijs, Patricia Verheugd, Bernhard Lüscher
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/827b3706279b44c7a5d83f1b4485f73c
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:827b3706279b44c7a5d83f1b4485f73c
record_format	dspace
spelling	oai:doaj.org-article:827b3706279b44c7a5d83f1b4485f73c2021-12-02T15:07:49ZNucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription10.1038/s41598-018-25137-w2045-2322https://doaj.org/article/827b3706279b44c7a5d83f1b4485f73c2018-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-25137-whttps://doaj.org/toc/2045-2322Abstract 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.Mareike BütepageChristian PreisingerAlexander von KriegsheimAnja ScheufenEva LausbergJinyu LiFerdinand KappesRegina FeederleSabrina ErnstLaura EckeiSarah KriegGerhard Müller-NewenGiulia RossettiKarla L. H. FeijsPatricia VerheugdBernhard LüscherNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-17 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mareike Bütepage Christian Preisinger Alexander von Kriegsheim Anja Scheufen Eva Lausberg Jinyu Li Ferdinand Kappes Regina Feederle Sabrina Ernst Laura Eckei Sarah Krieg Gerhard Müller-Newen Giulia Rossetti Karla L. H. Feijs Patricia Verheugd Bernhard Lüscher Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
description	Abstract 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.
format	article
author	Mareike Bütepage Christian Preisinger Alexander von Kriegsheim Anja Scheufen Eva Lausberg Jinyu Li Ferdinand Kappes Regina Feederle Sabrina Ernst Laura Eckei Sarah Krieg Gerhard Müller-Newen Giulia Rossetti Karla L. H. Feijs Patricia Verheugd Bernhard Lüscher
author_facet	Mareike Bütepage Christian Preisinger Alexander von Kriegsheim Anja Scheufen Eva Lausberg Jinyu Li Ferdinand Kappes Regina Feederle Sabrina Ernst Laura Eckei Sarah Krieg Gerhard Müller-Newen Giulia Rossetti Karla L. H. Feijs Patricia Verheugd Bernhard Lüscher
author_sort	Mareike Bütepage
title	Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
title_short	Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
title_full	Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
title_fullStr	Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
title_full_unstemmed	Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
title_sort	nucleolar-nucleoplasmic shuttling of targ1 and its control by dna damage-induced poly-adp-ribosylation and by nucleolar transcription
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/827b3706279b44c7a5d83f1b4485f73c
work_keys_str_mv	AT mareikebutepage nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT christianpreisinger nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT alexandervonkriegsheim nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT anjascheufen nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT evalausberg nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT jinyuli nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT ferdinandkappes nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT reginafeederle nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT sabrinaernst nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT lauraeckei nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT sarahkrieg nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT gerhardmullernewen nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT giuliarossetti nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT karlalhfeijs nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT patriciaverheugd nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription AT bernhardluscher nucleolarnucleoplasmicshuttlingoftarg1anditscontrolbydnadamageinducedpolyadpribosylationandbynucleolartranscription
_version_	1718388398623817728

Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription

Ejemplares similares