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Cell fate regulation by chromatin ADP-ribosylation


Abplanalp, Jeannette; Hottiger, Michael O (2017). Cell fate regulation by chromatin ADP-ribosylation. Seminars in Cell & Developmental Biology, 63:114-122.

Abstract

ADP-ribosylation is an evolutionarily conserved complex posttranslational modification that alters protein function and/or interaction. Intracellularly, it is mainly catalyzed by diphtheria toxin-like ADP-ribosyltransferases (ARTDs), which attach one or several ADP-ribose residues onto target proteins. Several specific mono- and poly-ADP-ribosylation binding modules exist; hydrolases reverse the modification. The best-characterized ARTD family member, ARTD1, regulates various DNA-associated processes. Here, we focus on the role of ARTD1-mediated chromatin ADP-ribosylation in development, differentiation, and pluripotency, and the recent development of new methodologies that will enable more insight into these processes.

Abstract

ADP-ribosylation is an evolutionarily conserved complex posttranslational modification that alters protein function and/or interaction. Intracellularly, it is mainly catalyzed by diphtheria toxin-like ADP-ribosyltransferases (ARTDs), which attach one or several ADP-ribose residues onto target proteins. Several specific mono- and poly-ADP-ribosylation binding modules exist; hydrolases reverse the modification. The best-characterized ARTD family member, ARTD1, regulates various DNA-associated processes. Here, we focus on the role of ARTD1-mediated chromatin ADP-ribosylation in development, differentiation, and pluripotency, and the recent development of new methodologies that will enable more insight into these processes.

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Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:05 Vetsuisse Faculty > Department of Molecular Mechanisms of Disease
07 Faculty of Science > Department of Molecular Mechanisms of Disease
Dewey Decimal Classification:570 Life sciences; biology
Uncontrolled Keywords:ADP-ribosylation, ARTD, Chromatin, Differentiation, Histone, PARP, Pluripotency
Language:English
Date:2017
Deposited On:30 Jan 2017 11:27
Last Modified:19 Feb 2018 07:35
Publisher:Elsevier
ISSN:1084-9521
OA Status:Closed
Publisher DOI:https://doi.org/10.1016/j.semcdb.2016.09.010
PubMed ID:27693398

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