Established that CATSPERZ is a bona fide subunit of the CatSper complex and defined its role in organizing the channel's nanodomain architecture rather than carrying the pore.
Evidence Knockout mouse with CatSper current electrophysiology, STORM super-resolution imaging of flagellar nanodomains, and rheotaxis/IVF assays
- Molecular mechanism by which CATSPERZ enforces the ~0.8 μm quadrilateral nanodomain spacing is unresolved
- Direct physical interactions with specific CatSper subunits not mapped
- No structural model of how CATSPERZ integrates into the channel complex