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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 
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 
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 
GenomicsGenome-wide screen of Mycobacterium tuberculosis-infected macrophages revealed GID/CTLH complex-mediated modulation of bacterial growth
Genome-wide screen of Mycobacterium tuberculosis-infected macrophages revealed GID/CTLH complex-mediated modulation of bacterial growth
PRJNA1109426 | ENA
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 
TranscriptomicsGenome-wide screen of Mycobacterium tuberculosis-infected macrophages revealed GID/CTLH complex-mediated modulation of bacterial growth
The eukaryotic GID/CTLH complex is a highly conserved E3 ubiquitin ligase involved in a broad range of biological processes. However, a role of this complex in host antimicrobial defenses has not been described. We exploited Mycobacterium tuberculosis (Mtb) induced cytotoxicity in macrophages in a F...
ORGANISM(S): Mycobacterium tuberculosis Mus musculus 
2024-05-08 | GSE267063 | GEO
GenomicsUbiquitylation by the GID/CTLH complex regulates the metabolic and innate immune response of macrophages to infection by Mycobacterium tuberculosis
Ubiquitylation by the GID/CTLH complex regulates the metabolic and innate immune response of macrophages to infection by Mycobacterium tuberculosis
PRJNA1438494 | ENA
TranscriptomicsUbiquitylation 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 an...
ORGANISM(S): Mus musculus 
2026-03-18 | GSE325061 | GEO
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 
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