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- W4386135412 abstract "Radial spokes (RS) are T-shaped multiprotein complexes on the axonemal microtubules. Repeated RS1, RS2, and RS3 couple the central pair to modulate ciliary and flagellar motility. Despite the cell type specificity of RS3 substructures, their molecular components remain largely unknown. Here, we report that a leucine-rich repeat-containing protein, LRRC23, is an RS3 head component essential for its head assembly and flagellar motility in mammalian spermatozoa. From infertile male patients with defective sperm motility, we identified a splice site variant of LRRC23. A mutant mouse model mimicking this variant produces a truncated LRRC23 at the C-terminus that fails to localize to the sperm tail, causing male infertility due to defective sperm motility. LRRC23 was previously proposed to be an ortholog of the RS stalk protein RSP15. However, we found that purified recombinant LRRC23 interacts with an RS head protein RSPH9, which is abolished by the C-terminal truncation. Our comparative sequence analyses also showed that LRRC34, not LRRC23, is the RSP15 ortholog. Cryo-electron tomography clearly revealed that the absence of the RS3 head and the sperm-specific RS2-RS3 bridge structure in LRRC23 mutant spermatozoa. Our study provides new insights into the structure and function of RS3 in mammalian spermatozoa and the molecular pathogenicity of LRRC23 underlying reduced sperm motility in infertile human males." @default.
- W4386135412 created "2023-08-25" @default.
- W4386135412 date "2023-08-24" @default.
- W4386135412 modified "2023-09-27" @default.
- W4386135412 title "Reviewer #1 (Public Review): LRRC23 truncation impairs radial spoke 3 head assembly and sperm motility underlying male infertility" @default.
- W4386135412 doi "https://doi.org/10.7554/elife.90095.1.sa1" @default.
- W4386135412 hasPublicationYear "2023" @default.
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