Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C

Andrej Paluda; Adam J. Middleton; Claudia Rossig; Peter D. Mace; Catherine L. Day

doi:10.1038/s41467-022-28782-y

Nature Communications (Mar 2022)

Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C

Andrej Paluda,
Adam J. Middleton,
Claudia Rossig,
Peter D. Mace,
Catherine L. Day

Affiliations

Andrej Paluda: Biochemistry Department, School of Biomedical Sciences, University of Otago
Adam J. Middleton: Biochemistry Department, School of Biomedical Sciences, University of Otago
Claudia Rossig: Biochemistry Department, School of Biomedical Sciences, University of Otago
Peter D. Mace: Biochemistry Department, School of Biomedical Sciences, University of Otago
Catherine L. Day: Biochemistry Department, School of Biomedical Sciences, University of Otago

DOI: https://doi.org/10.1038/s41467-022-28782-y
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 12

Abstract

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Attachment of ubiquitin to proteins is tightly regulated and controls many signalling pathways. Here, the authors show that addition of ubiquitin by the RING E3 ligases Arkadia and Ark2C is enhanced by ubiquitin and a charged loop that precedes the RING domain.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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