Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation

Shuai Qiao; Chia-Wei Lee; Dawafuti Sherpa; Jakub Chrustowicz; Jingdong Cheng; Maximilian Duennebacke; Barbara Steigenberger; Ozge Karayel; Duc Tung Vu; Susanne von Gronau; Matthias Mann; Florian Wilfling; Brenda A. Schulman

doi:10.1038/s41467-022-30803-9

Nature Communications (Jun 2022)

Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation

Shuai Qiao,
Chia-Wei Lee,
Dawafuti Sherpa,
Jakub Chrustowicz,
Jingdong Cheng,
Maximilian Duennebacke,
Barbara Steigenberger,
Ozge Karayel,
Duc Tung Vu,
Susanne von Gronau,
Matthias Mann,
Florian Wilfling,
Brenda A. Schulman

Affiliations

Shuai Qiao: Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry
Chia-Wei Lee: Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry
Dawafuti Sherpa: Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry
Jakub Chrustowicz: Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry
Jingdong Cheng: Institutes of Biomedical Sciences, Shanghai Key Laboratory of Medical Epigenetics, International Co-laboratory of Medical Epigenetics and Metabolism, University of Fudan
Maximilian Duennebacke: Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry
Barbara Steigenberger: Mass Spectrometry Core Facility, Max Planck Institute of Biochemistry
Ozge Karayel: Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry
Duc Tung Vu: Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry
Susanne von Gronau: Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry
Matthias Mann: Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry
Florian Wilfling: Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry
Brenda A. Schulman: Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry

DOI: https://doi.org/10.1038/s41467-022-30803-9
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 15

Abstract

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The GID E3 ligase regulates glucose-induced degradation in yeast, and key physiology. This study unveils E3 ligase regulation by reshaping the substrate binding site, blocking substrate access to ubiquitination active sites, and a Cage-like assembly.

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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