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TitleA proton-gated channel identified in the centipede antenna.
Journal, issue, pagesEMBO Rep, Vol. 26, Issue 24, Page 6083-6095, Year 2025
Publish dateOct 20, 2025
AuthorsWenqi Dong / Licheng Yuan / Jiangming Shang / Fan Yang / Shilong Yang / Xiancui Lu / Qian Wang / Anna Luo / Jiheng Geng / Jiatong Cheng / Runze Li / Yunfei Wang /
PubMed AbstractAcid sensing is essential for various biological processes in animals, yet it exhibits species-specific characteristics. In this study, we identified a proton-dissociation-permeated sodium channel ...Acid sensing is essential for various biological processes in animals, yet it exhibits species-specific characteristics. In this study, we identified a proton-dissociation-permeated sodium channel (PDPNaC1) in the antennal sensory neurons of the centipede Scolopendra subspinipes mutilans. PDPNaC1, which is permeable to monovalent cations, assembles as a homotrimer. Unlike most proton-gated channels, where proton binding induces currents, PDPNaC1's transient ion-permeable state is triggered by proton dissociation. By resolving the high-resolution cryo-electron microscopy (cryo-EM) structure of PDPNaC1, combined with mutagenesis and electrophysiological analyses, we identified Gly378, rather than the Gly-Ala-Ser tract, as a key determinant of ion selectivity. Furthermore, Ser376, located in the ion-permeable pathway, likely serves as a proton-binding site, leading to an H-blocking effect that results in proton-dissociated currents. Thus, the identification of PDPNaC1 suggests the remarkable diversity of proton responses and molecular mechanisms in DEG/ENaC family.
External linksEMBO Rep / PubMed:41116071 / PubMed Central
MethodsEM (single particle)
Resolution3.03 Å
Structure data

61429

9jf7

EMDB-61429, PDB-9jf7:
The structure of PDPNaC1 at APO state
Method: EM (single particle) / Resolution: 3.03 Å

Source
  • scolopendra mutilans (arthropod)
KeywordsMEMBRANE PROTEIN / PDPNaC1 / Trimer

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