Chaperonin TRiC bridges radial spokes for folding locally translated proteins to sustain mammalian sperm flagellar motility - PubMed
4 hours ago
- #local translation
- #protein folding
- #sperm motility
- Chaperonin TRiC is located in a barrel structure (RRB) between radial spokes RS1 and RS2 in mammalian sperm flagella, which is not present in externally fertilizing species.
- TRiC in the RRB folds locally synthesized proteins within the flagellum to maintain motility, supported by cryo-EM and cryo-ET showing its active, substrate-receptive state.
- Mammalian flagella contain translation machinery for local protein synthesis, and cross-linking mass spectrometry identifies axonemal proteins as potential folding substrates.
- Inhibiting TRiC ATPase activity reduces mouse sperm motility, highlighting TRiC's crucial role in sustaining flagellar movement in internally fertilizing animals.