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TitleChaperonin TRiC bridges radial spokes for folding locally translated proteins to sustain mammalian sperm flagellar motility.
Journal, issue, pagesMol Cell, Vol. 86, Issue 7, Page 1327-1344.e10, Year 2026
Publish dateApr 2, 2026
AuthorsXueming Meng / Luan Li / Cheng Lin / Yun Zhu / Yanyan Feng / Qun Zhao / Nan Zhao / Xuehai Zhou / Yujie Tong / Shanshan Wang / Guoliang Yin / Ruimin Liu / Lihua Zhang / Fei Sun / Xiumin Yan / Xueliang Zhu / Yao Cong /
PubMed AbstractAs animals evolved from external to internal fertilization, sperm flagella, once transiently propelling sperm in water to reach nearby eggs, developed to beat for days in the viscous female ...As animals evolved from external to internal fertilization, sperm flagella, once transiently propelling sperm in water to reach nearby eggs, developed to beat for days in the viscous female reproductive tract. How flagella are remodeled accordingly remains unclear. Unlike externally fertilizing zebrafish and sea urchins, mammalian flagella feature a barrel between radial spokes (RSs) RS1 and RS2. Here, we show that this RS1-RS2 barrel (RRB) is a unique T-complex protein-1 ring complex (TRiC) that folds locally translated polypeptides to sustain flagellar motility. Cryo-electron microscopy (cryo-EM) reveals a flagellum-specific TRiC structure. An in situ cryo-electron tomography (cryo-ET) map of flagellar axonemes captures the RRB TRiC in an active, substrate-receptive state, with additional densities suggestive of folding substrates and cofactors. Mammalian flagella contain components of translation machineries and locally synthesize proteins. Cross-linking mass spectrometry identifies candidate locally translated axonemal proteins and folding substrates. Furthermore, a TRiC ATPase inhibitor markedly represses mouse sperm motility. Our findings provide insights into flagellar remodeling in internally fertilizing species.
External linksMol Cell / PubMed:41932310
MethodsEM (single particle)
Resolution3.39 - 4.14 Å
Structure data

EMDB-62230: TRiC purified from bovine sperm flagella, concensus map
Method: EM (single particle) / Resolution: 3.59 Å

EMDB-62231: TRiC purified from bovine flagellar, focused refinement on E-domain
Method: EM (single particle) / Resolution: 3.39 Å

EMDB-62236: TRiC from bovine flagella, focused refinement on one-ring
Method: EM (single particle) / Resolution: 4.14 Å

62249

9kcf

EMDB-62249, PDB-9kcf:
Bovine Flagellar TRiC
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • bos taurus (domestic cattle)
KeywordsCHAPERONE / TRiC / sperm / flagella / motile cilia

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