The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1

Adam J. Middleton; Rhesa Budhidarmo; Anubrita Das; Jingyi Zhu; Martina Foglizzo; Peter D. Mace; Catherine L. Day

doi:10.1038/s41467-017-01665-3

Nature Communications (Nov 2017)

The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1

Adam J. Middleton,
Rhesa Budhidarmo,
Anubrita Das,
Jingyi Zhu,
Martina Foglizzo,
Peter D. Mace,
Catherine L. Day

Affiliations

Adam J. Middleton: Department of Biochemistry, School of Biomedical Sciences, University of Otago
Rhesa Budhidarmo: Department of Biochemistry, School of Biomedical Sciences, University of Otago
Anubrita Das: Department of Biochemistry, School of Biomedical Sciences, University of Otago
Jingyi Zhu: Department of Biochemistry, School of Biomedical Sciences, University of Otago
Martina Foglizzo: Department of Biochemistry, School of Biomedical Sciences, University of Otago
Peter D. Mace: Department of Biochemistry, School of Biomedical Sciences, University of Otago
Catherine L. Day: Department of Biochemistry, School of Biomedical Sciences, University of Otago

DOI: https://doi.org/10.1038/s41467-017-01665-3
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 10

Abstract

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TRAF6 is a RING E3 ligase that builds Lys63-linked ubiquitin chains. Here, the authors present the crystal structure of TRAF6 bound to the Ubc13~Ub conjugate, which, together with biochemical assays, reveals the role of the zinc finger domains and why RING dimerisation is required for TRAF6 activity.

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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