3D structure and in situ arrangements of CatSper channel in the sperm flagellum

Yanhe Zhao, Huafeng Wang, Caroline Wiesehoefer, Naman B. Shah, Evan Reetz, Jae Yeon Hwang, Xiaofang Huang, Tse-en Wang, Polina V. Lishko, Karen M. Davies, Gunther Wennemuth, Daniela Nicastro () and Jean-Ju Chung ()
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Yanhe Zhao: University of Texas Southwestern Medical Center
Huafeng Wang: Yale School of Medicine
Caroline Wiesehoefer: University of Duisburg-Essen, Medical Faculty
Naman B. Shah: University of California
Evan Reetz: University of Texas Southwestern Medical Center
Jae Yeon Hwang: Yale School of Medicine
Xiaofang Huang: Yale School of Medicine
Tse-en Wang: Yale School of Medicine
Polina V. Lishko: University of California
Karen M. Davies: University of California
Gunther Wennemuth: University of Duisburg-Essen, Medical Faculty
Daniela Nicastro: University of Texas Southwestern Medical Center
Jean-Ju Chung: Yale School of Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract The sperm calcium channel CatSper plays a central role in successful fertilization as a primary Ca2+ gateway. Here, we applied cryo-electron tomography to visualize the higher-order organization of the native CatSper complex in intact mammalian sperm. The repeating CatSper units form long zigzag-rows along mouse and human sperm flagella. Above each tetrameric channel pore, most of the extracellular domains form a canopy that interconnects to a zigzag-shaped roof. Murine CatSper contains an additional wing-structure connected to the tetrameric channel. The intracellular domains link two neighboring channels to a diagonal array, suggesting a dimer formation. Fitting of an atomic model of isolated monomeric CatSper to the in situ map reveals supramolecular interactions and assembly of the CatSper complex. Loss of EFCAB9-CATSPERζ alters the architecture and interactions of the channels, resulting in fragmentation and misalignment of the zigzag-rows and disruption of flagellar movement in Efcab9−/− sperm. This work offers unique insights into the structural basis for understanding CatSper regulation of sperm motility.

Date: 2022
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DOI: 10.1038/s41467-022-31050-8

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