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ProteomicsCryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation
Protein degradation, a major eukaryotic response to cellular signals, is subject to numerous layers of regulation. In yeast, the evolutionarily conserved GID E3 ligase mediates glucose-induced degradation of fructose-1,6-bisphosphatase (Fbp1) and other gluconeogenic enzymes. “GID” is a collection of...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-05-29 | PXD028579 | Pride
Gid E3 ligase complex Crzoem 
ProteomicsCryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation
Protein degradation, a major eukaryotic response to cellular signals, is subject to numerous layers of regulation. In yeast, the evolutionarily conserved GID E3 ligase mediates glucose-induced degradation of fructose-1,6-bisphosphatase (Fbp1) and other gluconeogenic enzymes. “GID” is a collection of...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-06-01 | PXD031713 | Pride
Gid e3 Proteomics Mass spectrometry Ubiquitination E3 ligase 
Proteomics1A GID E3 ligase assembly ubiquitinates an Rsp5 E3 adaptor and regulates plasma membrane transporters
Cells rapidly remodel their proteomes to align their cellular metabolism to environmentalconditions. Ubiquitin E3 ligases enablethis response, by facilitatingrapid andreversible changes to protein stability, localization, or interaction partners. In S. cerevisiae, the GID E3 ligase ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-03-02 | PXD030902 | Pride
Gid Proteomics Nutrient signaling Dia Ms Ubiquitin e3 ligase Metabolism Rsp5 
UnknownA GID E3 ligase assembly ubiquitinates an Rsp5 E3 adaptor and regulates plasma membrane transporters.
Not available
S-EPMC9171410 | biostudies-literature
UnknownMultisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies.
Not available
S-EPMC10843684 | biostudies-literature
ProteomicsGID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme
How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex, mutation of which is Glucose-Induced Degradation deficient, we discover supramolecular chelate assembly as an E3 ligase strategy for targeting an oligomeric substrate. Cryo EM s...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-04-28 | PXD024462 | Pride
Supramolecular assembly Metabolism Gluconeogenesis Cryo em E3 ligase Gid Ubiquitin Ctlh 
UnknownCryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation.
Not available
S-EPMC9160049 | biostudies-literature
UnknownStructural and Functional Insights into GID/CTLH E3 Ligase Complexes.
Not available
S-EPMC9180843 | biostudies-literature
UnknownThe multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation.
Not available
S-EPMC6037477 | biostudies-literature
UnknownGID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.
Not available
S-EPMC8189437 | biostudies-literature
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