Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase 
Conformations via Metabolically Driven Substrate Receptor Assembly

Qiao, Shuai; Langlois, Christine R.; Chrustowicz, Jakub; Sherpa, Dawafuti; Karayel, Ozge; Hansen, Fynn M.; Beier, Viola; von Gronau, Susanne; Bollschweiler, Daniel; Schäfer, Tillmann; Alpi, Arno F.; Mann, Matthias; Prabu, J. Rajan; Schulman, Brenda

doi:10.1016/j.molcel.2019.10.009

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Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly

MPS-Authors

/persons/resource/persons240596

Qiao, Shuai
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons203515

Langlois, Christine R.
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons245081

Chrustowicz, Jakub
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons238966

Sherpa, Dawafuti
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons213408

Karayel, Ozge
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons245079

Hansen, Fynn M.
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons128408

Beier, Viola
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78034

von Gronau, Susanne
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons179813

Bollschweiler, Daniel
Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons238712

Schäfer, Tillmann
Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77672

Alpi, Arno F.
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons78356

Mann, Matthias
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons131140

Prabu, J. Rajan
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons213292

Schulman, Brenda
Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society;

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引用

Qiao, S., Langlois, C. R., Chrustowicz, J., Sherpa, D., Karayel, O., Hansen, F. M., Beier, V., von Gronau, S., Bollschweiler, D., Schäfer, T., Alpi, A. F., Mann, M., Prabu, J. R., & Schulman, B. (2020). Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly. MOLECULAR CELL, 77(1), 150-163.e9. doi:10.1016/j.molcel.2019.10.009.

引用: https://hdl.handle.net/21.11116/0000-0005-A11A-8

要旨

Cells respond to environmental changes by toggling metabolic pathways, preparing for homeostasis, and anticipating future stresses. For example, in Saccharomyces cerevisiae, carbon stress-induced gluconeogenesis is terminated upon glucose availability, a process that involves the multiprotein E3 ligase GID(SR4) recruiting N termini and catalyzing ubiquitylation of gluconeogenic enzymes. Here, genetics, biochemistry, and cryoelectron microscopy define molecular underpinnings of glucose-induced degradation. Unexpectedly, carbon stress induces an inactive anticipatory complex (GID(Ant)), which awaits a glucose-induced substrate receptor to form the active GID(SR4). Meanwhile, other environmental perturbations elicit production of an alternative substrate receptor assembling into a related E3 ligase complex. The intricate structure of GID(Ant) enables anticipating and ultimately binding various N-degron-targeting (i.e., "N-end rule") substrate receptors, while the GID(SR4 )E3 forms a clamp-like structure juxtaposing substrate lysines with the ubiquitylation active site. The data reveal evolutionarily conserved GID complexes as a family of multisubunit E3 ubiquitin ligases responsive to extracellular stimuli.