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

Research output: Contribution to journal › Journal article › Research › peer-review

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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, Tillman; Alpi, Arno F; Mann, Matthias; Prabu, J Rajan; Schulman, Brenda A.

In: Molecular Cell, 01.11.2019.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Qiao, S, Langlois, CR, Chrustowicz, J, Sherpa, D, Karayel, O, Hansen, FM, Beier, V, von Gronau, S, Bollschweiler, D, Schäfer, T, Alpi, AF, Mann, M, Prabu, JR & Schulman, BA 2019, 'Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly', Molecular Cell. https://doi.org/10.1016/j.molcel.2019.10.009

APA

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. A. (2019). Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly. Molecular Cell. https://doi.org/10.1016/j.molcel.2019.10.009

Vancouver

Qiao S, Langlois CR, Chrustowicz J, Sherpa D, Karayel O, Hansen FM et al. Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly. Molecular Cell. 2019 Nov 1. https://doi.org/10.1016/j.molcel.2019.10.009

Author

Qiao, Shuai ; Langlois, Christine R ; Chrustowicz, Jakub ; Sherpa, Dawafuti ; Karayel, Ozge ; Hansen, Fynn M ; Beier, Viola ; von Gronau, Susanne ; Bollschweiler, Daniel ; Schäfer, Tillman ; Alpi, Arno F ; Mann, Matthias ; Prabu, J Rajan ; Schulman, Brenda A. / Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly. In: Molecular Cell. 2019.

Bibtex

@article{b91f06e6242a450cb54b282ad8301a09,
title = "Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly",
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 GIDSR4 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 (GIDAnt), which awaits a glucose-induced substrate receptor to form the active GIDSR4. Meanwhile, other environmental perturbations elicit production of an alternative substrate receptor assembling into a related E3 ligase complex. The intricate structure of GIDAnt enables anticipating and ultimately binding various N-degron-targeting (i.e., {"}N-end rule{"}) substrate receptors, while the GIDSR4 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.",
author = "Shuai Qiao and Langlois, {Christine R} and Jakub Chrustowicz and Dawafuti Sherpa and Ozge Karayel and Hansen, {Fynn M} and Viola Beier and {von Gronau}, Susanne and Daniel Bollschweiler and Tillman Sch{\"a}fer and Alpi, {Arno F} and Matthias Mann and Prabu, {J Rajan} and Schulman, {Brenda A}",
note = "Copyright {\textcopyright} 2019 Elsevier Inc. All rights reserved.",
year = "2019",
month = nov,
day = "1",
doi = "10.1016/j.molcel.2019.10.009",
language = "English",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",

}

RIS

TY - JOUR

T1 - Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly

AU - Qiao, Shuai

AU - Langlois, Christine R

AU - Chrustowicz, Jakub

AU - Sherpa, Dawafuti

AU - Karayel, Ozge

AU - Hansen, Fynn M

AU - Beier, Viola

AU - von Gronau, Susanne

AU - Bollschweiler, Daniel

AU - Schäfer, Tillman

AU - Alpi, Arno F

AU - Mann, Matthias

AU - Prabu, J Rajan

AU - Schulman, Brenda A

N1 - Copyright © 2019 Elsevier Inc. All rights reserved.

PY - 2019/11/1

Y1 - 2019/11/1

N2 - 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 GIDSR4 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 (GIDAnt), which awaits a glucose-induced substrate receptor to form the active GIDSR4. Meanwhile, other environmental perturbations elicit production of an alternative substrate receptor assembling into a related E3 ligase complex. The intricate structure of GIDAnt enables anticipating and ultimately binding various N-degron-targeting (i.e., "N-end rule") substrate receptors, while the GIDSR4 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.

AB - 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 GIDSR4 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 (GIDAnt), which awaits a glucose-induced substrate receptor to form the active GIDSR4. Meanwhile, other environmental perturbations elicit production of an alternative substrate receptor assembling into a related E3 ligase complex. The intricate structure of GIDAnt enables anticipating and ultimately binding various N-degron-targeting (i.e., "N-end rule") substrate receptors, while the GIDSR4 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.

U2 - 10.1016/j.molcel.2019.10.009

DO - 10.1016/j.molcel.2019.10.009

M3 - Journal article

C2 - 31708416

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

ER -

ID: 230143911