Sort   by:  
 Page size 
ProteomicsThe GID Ubiquitin Ligase Complex is a Regulator of AMPK Activity and Organismal Lifespan
The AMP-activated protein kinase (AMPK) regulates cellular energy homeostasis by sensing the metabolic status of the cell. AMPK is regulated by phosphorylation and dephosphorylation as a result of changing AMP/ATP levels and by removal of inhibitory ubiquitin residues by USP10. In this context, we i...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-08 | PXD015170 | Pride
Ampk  autophagy  gid  longevity  mtor  primary cilium  ubiquitination 
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 
ProteomicsUbiquitylation by the GID/CTLH complex regulates the metabolic and innate immune response of macrophages to infection by Mycobacterium tuberculosis
The GID/CTLH E3 ligase complex is implicated in several biological processes, yet its full substrate repertoire remains poorly defined. We recently identified the complex as a broad modulator of macrophage responses to Mycobacterium tuberculosis (Mtb) infection. Here, we use label-free proteomics a...
ORGANISM(S): Mus musculus (Mouse) 
2026-06-24 | PXD075792 | Pride
Metabolism Innate immunity Ubiquitylation Tuberculosis Gid/ctlh complex Macrophages 
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 
GenomicsBidirectional control of a metabolic transition by the GID ubiquitin ligase
Bidirectional control of a metabolic transition by the GID ubiquitin ligase
PRJNA1289760 | ENA
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 
ProteomicsThe human GID complex engages two independent modules for substrate recruitment
Chemical cross-linking coupled to mass spectrometry was used to study two different assemblies of the human E3 ubiquitin ligase complex, GID. The 5mer complex consisted of subunits MAEA, RMND5a, TWA1, WDR26, and RanBP9; the 6mer complex consisted of the subunits of the 5mer complex and the additiona...
ORGANISM(S): Homo sapiens (Human) 
2021-08-25 | PXD024822 | Pride
Chemical cross-linking  dss  pdh  dmtmm  structural proteomics  gid complex 
OtherBidirectional control of a metabolic transition by the GID ubiquitin ligase
The GID/CTLH ubiquitin ligase is a multisubunit E3 conserved across eukaryotes. GID/CTLH has been implicated in a variety of processes, including metabolic regulation, cell proliferation, embryonic development and cell differentiation. However, our understanding of substrate recognition by GID/CTLH ...
ORGANISM(S): Saccharomyces cerevisiae 
2026-07-10 | GSE302269 | GEO
UnknownThe life sciences Global Image Database (GID).
Not available
S-EPMC29843 | 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 
Sort   by:  
 Page size