ArticleNature communications2026
Structural basis of lipid-dependent allosteric gating mechanisms for PC1-PC2 ion channel.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Structural insights into ligand recognition and activation of the human oxoglutarate receptor OXGR1.Nature communications · 2026Article
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Authors and funding
15 authors.
Funding
Abstract
The polycystin complex, consisting of one polycystin-1 (PC1) and three polycystin-2 (PC2), forms a cation channel localized to the primary cilium and is critically involved in autosomal dominant polycystic kidney disease (ADPKD). This study reveals an allosteric gating mechanism of the PC1-PC2 channel modulated by specific membrane lipids. In typical membrane environments, phosphatidylglycerol (PG) and phosphatidic acid (PA) bind to the channel central pore, maintaining it in a closed state. Dissociation of these lipids transitions the channel to a pre-open state. The cilia-enriched oxysterol 7β,27-dihydroxycholesterol (7β,27-DHC) stabilizes the channel in a more open but still non-conductive conformation through an allosteric mechanism. Lipid-mediated regulation is coupled to large conformational rearrangements of the TOP and voltage-sensor-like domains (VSDs) of the third PC2 subunit, which eventually leads to pore opening. This lipid-dependent modulation is also observed in a gain-of-function channel. These findings reveal a distinct gating mechanism for the asymmetric 1:3 PC1-PC2 complex.
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