2025/02/10 by Alan Brown, Miguel Ricardo Leung, Tzviya Zeev‐Ben‐Mordehai +1 · 1 voice
Biochemistry, Genetics and Molecular Biology · #Heat shock proteins research #Microtubule and mitosis dynamics #Nuclear Structure and Function
paper · pdf · doi:10.1002/cm.22005
openalex publication_date 2025/02/10 · openalex created_date 2025/02/11 · openalex updated_date 2026/07/27
The TRiC chaperonin is responsible for folding ~5%-10% of the proteome in eukaryotic cells. Our recent cryo-electron microscopy studies of axonemes from diverse mammalian cell types led to the surprising discovery that a fully assembled TRiC chaperonin is a structural component of mammalian sperm flagella, where it is tethered to the radial spokes of doublet microtubules. In contrast, axoneme-tethered TRiC is not observed in mammalian epithelial cilia, nor in any of the non-mammalian sperm flagella studied to date. In this Perspective, we explore several hypotheses for the potential functions of axoneme-tethered TRiC in mature sperm.