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Cryo-EM structure of the 48-nm repeat doublet microtubule from mouse sperm
Structural highlights
FunctionCFA95_MOUSE Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.[UniProtKB:Q32L77] Publication Abstract from PubMedSperm motility is crucial for successful fertilization. Highly decorated doublet microtubules (DMTs) form the sperm tail skeleton, which propels the movement of spermatozoa. Using cryo-electron microscopy (cryo-EM) and artificial intelligence (AI)-based modeling, we determined the structures of mouse and human sperm DMTs and built an atomic model of the 48-nm repeat of the mouse sperm DMT. Our analysis revealed 47 DMT-associated proteins, including 45 microtubule inner proteins (MIPs). We identified 10 sperm-specific MIPs, including seven classes of Tektin5 in the lumen of the A tubule and FAM166 family members that bind the intra-tubulin interfaces. Interestingly, the human sperm DMT lacks some MIPs compared with the mouse sperm DMT. We also discovered variants in 10 distinct MIPs associated with a subtype of asthenozoospermia characterized by impaired sperm motility without evident morphological abnormalities. Our study highlights the conservation and tissue/species specificity of DMTs and expands the genetic spectrum of male infertility. Structures of sperm flagellar doublet microtubules expand the genetic spectrum of male infertility.,Zhou L, Liu H, Liu S, Yang X, Dong Y, Pan Y, Xiao Z, Zheng B, Sun Y, Huang P, Zhang X, Hu J, Sun R, Feng S, Zhu Y, Liu M, Gui M, Wu J Cell. 2023 Jun 22;186(13):2897-2910.e19. doi: 10.1016/j.cell.2023.05.009. Epub , 2023 Jun 8. PMID:37295417[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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