Proteomics

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Shulin packages axonemal outer dynein arms for ciliary targeting


ABSTRACT: The main force generators in eukaryotic cilia and flagella are axonemal outer dynein arms (ODAs). During cilio-genesis, these ∼1.8 MDa complexes are assembled in the cytoplasm and targeted to cilia via an unknown mechanism. Here we use the ciliate Tetrahymena to identify two novel factors (Q22YU3 and Q22MS1) which bind ODAs in the cytoplasm and are required for their delivery to cilia. We show that Q22YU3, which we name Shulin, locks the ODA motor domains into a closed conformation and inhibits motor activity. Cryo-EM reveals how Shulin stabilizes 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Tetrahymena Thermophila Cu428

SUBMITTER: Mark Skehel  

LAB HEAD: Andrew P Carter

PROVIDER: PXD022396 | Pride | 2021-09-09

REPOSITORIES: Pride

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Publications

Shulin packages axonemal outer dynein arms for ciliary targeting.

Mali Girish R GR   Ali Ferdos Abid FA   Lau Clinton K CK   Begum Farida F   Boulanger Jérôme J   Howe Jonathan D JD   Chen Zhuo A ZA   Rappsilber Juri J   Skehel Mark M   Carter Andrew P AP  

Science (New York, N.Y.) 20210201 6532


The main force generators in eukaryotic cilia and flagella are axonemal outer dynein arms (ODAs). During ciliogenesis, these ~1.8-megadalton complexes are assembled in the cytoplasm and targeted to cilia by an unknown mechanism. Here, we used the ciliate <i>Tetrahymena</i> 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  ...[more]

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