ion channel / membrane protein / calcium channel / protein complex / PROTEIN TRANSPORT
機能・相同性
機能・相同性情報
CatSper complex / Sperm Motility And Taxes / fusion of sperm to egg plasma membrane involved in single fertilization / sperm principal piece / regulation of cilium beat frequency involved in ciliary motility / calcium ion sensor activity / male meiotic nuclear division / organic anion transport / flagellated sperm motility / : ...CatSper complex / Sperm Motility And Taxes / fusion of sperm to egg plasma membrane involved in single fertilization / sperm principal piece / regulation of cilium beat frequency involved in ciliary motility / calcium ion sensor activity / male meiotic nuclear division / organic anion transport / flagellated sperm motility / : / calcium-activated cation channel activity / fertilization / motile cilium / sodium ion transport / sperm capacitation / regulation of calcium ion transport / monoatomic ion channel complex / sperm flagellum / voltage-gated calcium channel activity / acrosomal vesicle / bioluminescence / generation of precursor metabolites and energy / establishment of localization in cell / calcium ion transport / spermatogenesis / cell differentiation / calmodulin binding / cilium / calcium ion binding / endoplasmic reticulum / plasma membrane / cytoplasm 類似検索 - 分子機能
ジャーナル: Nature / 年: 2021 タイトル: Structure of a mammalian sperm cation channel complex. 著者: Shiyi Lin / Meng Ke / Yuqi Zhang / Zhen Yan / Jianping Wu / 要旨: The cation channel of sperm (CatSper) is essential for sperm motility and fertility. CatSper comprises the pore-forming proteins CATSPER1-4 and multiple auxiliary subunits, including CATSPERβ, γ, ...The cation channel of sperm (CatSper) is essential for sperm motility and fertility. CatSper comprises the pore-forming proteins CATSPER1-4 and multiple auxiliary subunits, including CATSPERβ, γ, δ, ε, ζ, and EFCAB9. Here we report the cryo-electron microscopy (cryo-EM) structure of the CatSper complex isolated from mouse sperm. In the extracellular view, CATSPER1-4 conform to the conventional domain-swapped voltage-gated ion channel fold, following a counterclockwise arrangement. The auxiliary subunits CATSPERβ, γ, δ and ε-each of which contains a single transmembrane segment and a large extracellular domain-constitute a pavilion-like structure that stabilizes the entire complex through interactions with CATSPER4, 1, 3 and 2, respectively. Our EM map reveals several previously uncharacterized components, exemplified by the organic anion transporter SLCO6C1. We name this channel-transporter ultracomplex the CatSpermasome. The assembly and organization details of the CatSpermasome presented here lay the foundation for the development of CatSpermasome-related treatments for male infertility and non-hormonal contraceptives.