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Readers of poly(ADP-ribose): designed to be fit for purpose

Post-translational modifications (PTMs) regulate many aspects of protein function and are indispensable for the spatio-temporal regulation of cellular processes. The proteome-wide identification of PTM targets has made significant progress in recent years, as has the characterization of their writer...

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Detalles Bibliográficos
Autores principales: Teloni, Federico, Altmeyer, Matthias
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4756826/
https://www.ncbi.nlm.nih.gov/pubmed/26673700
http://dx.doi.org/10.1093/nar/gkv1383
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author Teloni, Federico
Altmeyer, Matthias
author_facet Teloni, Federico
Altmeyer, Matthias
author_sort Teloni, Federico
collection PubMed
description Post-translational modifications (PTMs) regulate many aspects of protein function and are indispensable for the spatio-temporal regulation of cellular processes. The proteome-wide identification of PTM targets has made significant progress in recent years, as has the characterization of their writers, readers, modifiers and erasers. One of the most elusive PTMs is poly(ADP-ribosyl)ation (PARylation), a nucleic acid-like PTM involved in chromatin dynamics, genome stability maintenance, transcription, cell metabolism and development. In this article, we provide an overview on our current understanding of the writers of this modification and their targets, as well as the enzymes that degrade and thereby modify and erase poly(ADP-ribose) (PAR). Since many cellular functions of PARylation are exerted through dynamic interactions of PAR-binding proteins with PAR, we discuss the readers of this modification and provide a synthesis of recent findings, which suggest that multiple structurally highly diverse reader modules, ranging from completely folded PAR-binding domains to intrinsically disordered sequence stretches, evolved as PAR effectors to carry out specific cellular functions.
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spelling pubmed-47568262016-02-18 Readers of poly(ADP-ribose): designed to be fit for purpose Teloni, Federico Altmeyer, Matthias Nucleic Acids Res Survey and Summary Post-translational modifications (PTMs) regulate many aspects of protein function and are indispensable for the spatio-temporal regulation of cellular processes. The proteome-wide identification of PTM targets has made significant progress in recent years, as has the characterization of their writers, readers, modifiers and erasers. One of the most elusive PTMs is poly(ADP-ribosyl)ation (PARylation), a nucleic acid-like PTM involved in chromatin dynamics, genome stability maintenance, transcription, cell metabolism and development. In this article, we provide an overview on our current understanding of the writers of this modification and their targets, as well as the enzymes that degrade and thereby modify and erase poly(ADP-ribose) (PAR). Since many cellular functions of PARylation are exerted through dynamic interactions of PAR-binding proteins with PAR, we discuss the readers of this modification and provide a synthesis of recent findings, which suggest that multiple structurally highly diverse reader modules, ranging from completely folded PAR-binding domains to intrinsically disordered sequence stretches, evolved as PAR effectors to carry out specific cellular functions. Oxford University Press 2016-02-18 2015-12-15 /pmc/articles/PMC4756826/ /pubmed/26673700 http://dx.doi.org/10.1093/nar/gkv1383 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Survey and Summary
Teloni, Federico
Altmeyer, Matthias
Readers of poly(ADP-ribose): designed to be fit for purpose
title Readers of poly(ADP-ribose): designed to be fit for purpose
title_full Readers of poly(ADP-ribose): designed to be fit for purpose
title_fullStr Readers of poly(ADP-ribose): designed to be fit for purpose
title_full_unstemmed Readers of poly(ADP-ribose): designed to be fit for purpose
title_short Readers of poly(ADP-ribose): designed to be fit for purpose
title_sort readers of poly(adp-ribose): designed to be fit for purpose
topic Survey and Summary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4756826/
https://www.ncbi.nlm.nih.gov/pubmed/26673700
http://dx.doi.org/10.1093/nar/gkv1383
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