TRiC Is a Structural Component of Mammalian Sperm Axonemes

Alan Brown; Miguel Ricardo Leung; Tzviya Zeev-Ben-Mordehai; Rui Zhang

doi:10.1002/cm.22005

TRiC Is a Structural Component of Mammalian Sperm Axonemes

Alan Brown
, Miguel Ricardo Leung^*
, Tzviya Zeev-Ben-Mordehai
, Rui Zhang

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic

Abstract

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.

Original language	English
Pages (from-to)	791-794
Number of pages	4
Journal	Cytoskeleton (Hoboken, N.J.)
Volume	82
Issue number	12
Early online date	10 Feb 2025
DOIs	https://doi.org/10.1002/cm.22005
Publication status	Published - Dec 2025

Bibliographical note

Publisher Copyright:
© 2025 The Author(s). Cytoskeleton published by Wiley Periodicals LLC.

Funding

This work was supported by Richard and Susan Smith Family Foundation, National Institutes of Health, Nederlandse Organisatie voor Wetenschappelijk Onderzoek. Funding:

Funders
Richard and Susan Smith Family Foundation
National Institutes of Health
Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Keywords

TRiC
axonemes
chaperonin
cryo-EM
sperm

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10.1002/cm.22005Licence: CC BY

Cytoskeleton - 2025 - Brown - TRiC Is a Structural Component of Mammalian Sperm AxonemesFinal published version, 616 KBLicence: CC BY

Cite this

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title = "TRiC Is a Structural Component of Mammalian Sperm Axonemes",

abstract = "The TRiC chaperonin is responsible for folding \textasciitilde{}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.",

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author = "Alan Brown and Leung, \{Miguel Ricardo\} and Tzviya Zeev-Ben-Mordehai and Rui Zhang",

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doi = "10.1002/cm.22005",

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AB - 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.

KW - TRiC

KW - axonemes

KW - chaperonin

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TRiC Is a Structural Component of Mammalian Sperm Axonemes

Abstract

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Keywords

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