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

Qiao, S., Langlois, C. R., Chrustowicz, J., Sherpa, D., Karayel, O., Hansen, F. M., et al. (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.

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 Creators:
Qiao, Shuai1, Author              
Langlois, Christine R.1, Author              
Chrustowicz, Jakub1, Author              
Sherpa, Dawafuti1, Author              
Karayel, Ozge2, Author              
Hansen, Fynn M.2, Author              
Beier, Viola1, Author              
von Gronau, Susanne1, Author              
Bollschweiler, Daniel3, Author              
Schäfer, Tillmann3, Author              
Alpi, Arno F.1, Author              
Mann, Matthias2, Author              
Prabu, J. Rajan1, Author              
Schulman, Brenda1, Author              
Affiliations:
1Schulman, Brenda / Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Max Planck Society, ou_2466699              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
3Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              

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Free keywords: END RULE PATHWAY; CATABOLITE DEGRADATION; STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; YEAST GENES; CRYO-EM; PROTEIN; COMPLEX; FRUCTOSE-1,6-BISPHOSPHATASE; MECHANISM
 Abstract: 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.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: 23
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: MOLECULAR CELL
Source Genre: Journal
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Publ. Info: 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 77 (1) Sequence Number: - Start / End Page: 150 - 163.e9 Identifier: ISSN: 1097-2765