ArticleNature communications2024
Structural basis for autoinhibition by the dephosphorylated regulatory domain of Ycf1.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Linker domain Ser-phosphorylation as a putative modulator for ABCB alkaloid transporters.Planta · 2026Review
- Structural and functional implications of phase separation of membrane protein LacY in Escherichia coli.Nature communications · 2026Article
- Structural Basis for Oxidized Glutathione Recognition by Yeast Cadmium Factor 1.Journal of the American Chemical Society · 2025Article
- Structure of a dimeric full-length ABC transporter.Nature communications · 2024Article
- Cryo-EM reveals a phosphorylated R-domain envelops the NBD1 catalytic domain in an ABC transporter.Life science alliance · 2024Article
- Genome-Wide Identification and Expression Analyses of the Thaumatin-Like Protein Gene Family inPlants (Basel, Switzerland) · 2024Article
- Structural insight into binding site access and ligand recognition by human ABCB1.bioRxiv : the preprint server for biology · 2024Article
- Inhibition and transport mechanisms of the ABC transporter hMRP5.Nature communications · 2024Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Yeast Cadmium Factor 1 (Ycf1) sequesters glutathione and glutathione-heavy metal conjugates into yeast vacuoles as a cellular detoxification mechanism. Ycf1 belongs to the C subfamily of ATP Binding Cassette (ABC) transporters characterized by long flexible linkers, notably the regulatory domain (R-domain). R-domain phosphorylation is necessary for activity, whereas dephosphorylation induces autoinhibition through an undefined mechanism. Because of its transient and dynamic nature, no structure of the dephosphorylated Ycf1 exists, limiting understanding of this R-domain regulation. Here, we capture the dephosphorylated Ycf1 using cryo-EM and show that the unphosphorylated R-domain indeed forms an ordered structure with an unexpected hairpin topology bound within the Ycf1 substrate cavity. This architecture and binding mode resemble that of a viral peptide inhibitor of an ABC transporter and the secreted bacterial WXG peptide toxins. We further reveal the subset of phosphorylation sites within the hairpin turn that drive the reorganization of the R-domain conformation, suggesting a mechanism for Ycf1 activation by phosphorylation-dependent release of R-domain mediated autoinhibition.
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