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ProteomicsDoa10/MARCH6 architecture interconnects E3 ligase activity with lipid-binding transmembrane channel to regulate SQLE
Transmembrane E3 ligases play crucial roles in homeostasis. Much protein and organelle quality control, and metabolic regulation, are determined by ER-resident MARCH6 E3 ligases, including Doa10 in yeast. Here, we present Doa10/MARCH6 structural analysis by cryo-EM and AlphaFold predictions, and a s...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD047499 | Pride
Ubiquitylation E3 ubiquitin ligases March6 Membrane proteins Doa10 Cryo-em Sqle 
UnknownSubstrate recognition mechanism of the endoplasmic reticulum-associated ubiquitin ligase Doa10.
Not available
S-EPMC10928120 | biostudies-literature
UnknownSubstrate recognition mechanism of the endoplasmic reticulum-associated ubiquitin ligase Doa10.
Not available
S-EPMC10802466 | biostudies-literature
GenomicsNt-acetylation independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases
Nt-acetylation independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases
PRJNA989617 | ENA
UnknownThe yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.
Not available
S-EPMC4411271 | biostudies-literature
UnknownElements of the ERAD ubiquitin ligase Doa10 regulating sequential poly-ubiquitylation of its targets.
Not available
S-EPMC9619350 | biostudies-literature
ProteomicsGlobal and protein-specific analysis reveals Nt-acetylation-independent turnover of SQE1 by Arabidopsis DOA10-like E3 ligases
The Acetylation-dependent (Ac/) N-degron pathway degrades proteins through recognition of their acetylated N-termini (Nt) by specific E3-ligases (Ac/N-recognins). To date, no Ac/N-recognins have been defined in plants. Here we use molecular, genetic, and multi-omics approaches to characterise potent...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2024-01-26 | PXD043217 | Pride
Erad Nt-acetylation Ac/n-degron pathway Sterol biosynthesis Proteolysis Ac/n-recognin N-terminomics 
UnknownAn unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme.
Not available
S-EPMC3121455 | biostudies-literature
TranscriptomicsNt-acetylation independent turnover of SQUALENE EPOXIDASE 1 by Arabidopsis DOA10-like E3 ligases
The Acetylation-dependent (Ac/) N-degron pathway degrades proteins through recognition of their acetylated N-termini (Nt) by E3-ligases called Ac/N-recognins. To date, specific Ac/N-recognins have not been defined in plants. Here we used molecular, genetic, and multi-omics approaches to characterise...
ORGANISM(S): Arabidopsis thaliana 
2023-11-13 | GSE236282 | GEO
UnknownDoa10/MARCH6 architecture interconnects E3 ligase activity with lipid-binding transmembrane channel to regulate SQLE.
Not available
S-EPMC10776854 | biostudies-literature
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