Journal
SCIENCE
Volume 371, Issue 6532, Pages 910-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abe0526
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Funding
- Medical Research Council, UK [MRC_UP_A025_1011]
- Wellcome Trust [WT210711, 218653/Z/19/Z, 103139]
- Deutsche Forschungsgemeinschaft [EXC 2008/1-390540038, 426290502]
- Wellcome Trust [218653/Z/19/Z] Funding Source: Wellcome Trust
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The protein Shulin binds to ODAs in the cytoplasm, inhibits their motor activity, stabilizes their compact form, and facilitates their delivery to the cilia, providing a molecular explanation for the process.
The main force generators in eukaryotic cilia and flagella are axonemal outer dynein arms (ODAs). During ciliogenesis, these similar to 1.8-megadalton complexes are assembled in the cytoplasm and targeted to cilia by an unknown mechanism. Here, we used the ciliate Tetrahymena to identify two factors (Q22YU3 and Q22MS1) that bind ODAs in the cytoplasm and are required for ODA delivery to cilia. Q22YU3, which we named Shulin, locked the ODA motor domains into a closed conformation and inhibited motor activity. Cryo-electron microscopy revealed how Shulin stabilized this compact form of ODAs by binding to the dynein tails. Our findings provide a molecular explanation for how newly assembled dyneins are packaged for delivery to the cilia.
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