Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases-Reference-Cited by-同舟云学术

Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases

Published:2020-09-18 Issue:38 Volume:6 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Chatrin Chatrin¹²^ORCID,Gabrielsen Mads¹^ORCID,Buetow Lori¹^ORCID,Nakasone Mark A.¹^ORCID,Ahmed Syed F.¹^ORCID,Sumpton David¹^ORCID,Sibbet Gary J.¹,Smith Brian O.³^ORCID,Huang Danny T.¹²^ORCID

Affiliation:

1. Cancer Research UK Beatson Institute, Garscube Estate, Switchback Road, Glasgow G61 1BD, UK.

2. Institute of Cancer Sciences, University of Glasgow, Glasgow G61 1QH, UK.

3. Institute of Molecular Cell and System Biology, University of Glasgow, Glasgow G12 8QQ, UK.

Abstract

The C-terminal RING and DTC domains of mammalian Deltex proteins catalyze ADP-ribosylation at the C terminus of ubiquitin.

Funder

H2020 European Research Council

Cancer Research UK

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference71 articles.

1. Post-translational modifications in signal integration

2. The Age of Crosstalk: Phosphorylation, Ubiquitination, and Beyond

3. Post-translational regulation of ubiquitin signaling

4. Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage

5. Loss of Tankyrase-Mediated Destruction of 3BP2 Is the Underlying Pathogenic Mechanism of Cherubism

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