<scp>TRiC</scp> Is a Structural Component of Mammalian Sperm Axonemes
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.
Authors
- Tzviya Zeev‐Ben‐Mordehai (ORCID: https://orcid.org/0000-0002-2571-550X)
- Miguel Ricardo Leung (ORCID: https://orcid.org/0000-0002-3348-1096)
- Alan P Brown (ORCID: https://orcid.org/0000-0002-0021-0476)
- Rui Zhang (ORCID: https://orcid.org/0000-0003-3159-9565)
Institutions
- Harvard University (US)
- Utrecht University (NL)
- Washington University in St. Louis (US)
- University Medical Center Utrecht (NL)
- Hubrecht Institute for Developmental Biology and Stem Cell Research (NL)
- Boston VA Research Institute (US)
Publication Details
- Journal
- Cytoskeleton
- Published
- 2025-02-10
- DOI
- https://doi.org/10.1002/cm.22005
- Citations
- 3
- Primary Topic
- Heat shock proteins research
- Type
- article
- Field-Weighted Citation Impact
- 2.42
Funders
- Richard and Susan Smith Family Foundation
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
- National Institutes of Health