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

Chatrin Chatrin, Mads Gabrielsen, Lori Buetow, Mark A. Nakasone, Syed Feroj Ahmed, David Sumpton, Gary Sibbet, Brian O. Smith, Danny T. Huang

2020Science Advances101 citationsDOIOpen Access PDF

Abstract

bound to the DTC domain to facilitate ADP-ribosylation of ubiquitin. This ubiquitin modification prevents its activation but is reversed by the linkage nonspecific deubiquitinases. Our study provides mechanistic insights into ADP-ribosylation of ubiquitin by Deltex E3s and will enable future studies directed at understanding the increasingly complex network of ubiquitin cross-talk.

Topics & Concepts

UbiquitinUbiquitin ligaseUbiquitin-Protein LigasesDeubiquitinating enzymeCell biologyBiochemistryBiologyChemistryGeneUbiquitin and proteasome pathwaysPARP inhibition in cancer therapyCalcium signaling and nucleotide metabolism
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