Cargando…

The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series

Poly(ADP-ribosyl)ation is a post-translational modification of proteins that is mediated by poly(ADP-ribose) polymerases (PARPs). Although the existence and nature of the nucleic acid-like molecule poly(ADP-ribose) (PAR) has been known for 40 years, understanding its biological functions—originally...

Descripción completa

Detalles Bibliográficos
Autores principales: Hakmé, Antoinette, Wong, Heng-Kuan, Dantzer, Françoise, Schreiber, Valérie
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2581850/
https://www.ncbi.nlm.nih.gov/pubmed/18927583
http://dx.doi.org/10.1038/embor.2008.191
_version_ 1782160647633502208
author Hakmé, Antoinette
Wong, Heng-Kuan
Dantzer, Françoise
Schreiber, Valérie
author_facet Hakmé, Antoinette
Wong, Heng-Kuan
Dantzer, Françoise
Schreiber, Valérie
author_sort Hakmé, Antoinette
collection PubMed
description Poly(ADP-ribosyl)ation is a post-translational modification of proteins that is mediated by poly(ADP-ribose) polymerases (PARPs). Although the existence and nature of the nucleic acid-like molecule poly(ADP-ribose) (PAR) has been known for 40 years, understanding its biological functions—originally thought to be only the regulation of chromatin superstructure when DNA is broken—is still the subject of intense research. Here, we review the mechanisms controlling the biosynthesis of this complex macromolecule and some of its main biological functions, with an emphasis on the most recent advances and hypotheses that have developed in this rapidly growing field.
format Text
id pubmed-2581850
institution National Center for Biotechnology Information
language English
publishDate 2008
publisher Nature Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-25818502009-11-01 The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series Hakmé, Antoinette Wong, Heng-Kuan Dantzer, Françoise Schreiber, Valérie EMBO Rep Review Article Poly(ADP-ribosyl)ation is a post-translational modification of proteins that is mediated by poly(ADP-ribose) polymerases (PARPs). Although the existence and nature of the nucleic acid-like molecule poly(ADP-ribose) (PAR) has been known for 40 years, understanding its biological functions—originally thought to be only the regulation of chromatin superstructure when DNA is broken—is still the subject of intense research. Here, we review the mechanisms controlling the biosynthesis of this complex macromolecule and some of its main biological functions, with an emphasis on the most recent advances and hypotheses that have developed in this rapidly growing field. Nature Publishing Group 2008-11 2008-10-17 /pmc/articles/PMC2581850/ /pubmed/18927583 http://dx.doi.org/10.1038/embor.2008.191 Text en Copyright © 2008, European Molecular Biology Organization
spellingShingle Review Article
Hakmé, Antoinette
Wong, Heng-Kuan
Dantzer, Françoise
Schreiber, Valérie
The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series
title The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series
title_full The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series
title_fullStr The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series
title_full_unstemmed The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series
title_short The expanding field of poly(ADP-ribosyl)ation reactions. ‘Protein Modifications: Beyond the Usual Suspects' Review Series
title_sort expanding field of poly(adp-ribosyl)ation reactions. ‘protein modifications: beyond the usual suspects' review series
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2581850/
https://www.ncbi.nlm.nih.gov/pubmed/18927583
http://dx.doi.org/10.1038/embor.2008.191
work_keys_str_mv AT hakmeantoinette theexpandingfieldofpolyadpribosylationreactionsproteinmodificationsbeyondtheusualsuspectsreviewseries
AT wonghengkuan theexpandingfieldofpolyadpribosylationreactionsproteinmodificationsbeyondtheusualsuspectsreviewseries
AT dantzerfrancoise theexpandingfieldofpolyadpribosylationreactionsproteinmodificationsbeyondtheusualsuspectsreviewseries
AT schreibervalerie theexpandingfieldofpolyadpribosylationreactionsproteinmodificationsbeyondtheusualsuspectsreviewseries
AT hakmeantoinette expandingfieldofpolyadpribosylationreactionsproteinmodificationsbeyondtheusualsuspectsreviewseries
AT wonghengkuan expandingfieldofpolyadpribosylationreactionsproteinmodificationsbeyondtheusualsuspectsreviewseries
AT dantzerfrancoise expandingfieldofpolyadpribosylationreactionsproteinmodificationsbeyondtheusualsuspectsreviewseries
AT schreibervalerie expandingfieldofpolyadpribosylationreactionsproteinmodificationsbeyondtheusualsuspectsreviewseries