Shulin packages axonemal outer dynein arms for ciliary targeting

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 to identify two factors (Q22YU3 and Q22MS1) t...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2021-02, Vol.371 (6532), p.910-916
Main Authors: Mali, Girish R, Ali, Ferdos Abid, Lau, Clinton K, Begum, Farida, Boulanger, Jérôme, Howe, Jonathan D, Chen, Zhuo A, Rappsilber, Juri, Skehel, Mark, Carter, Andrew P
Format: Article
Language:English
Subjects:
Axonemal Dyneins - chemistry
Axonemal Dyneins - genetics
Axonemal Dyneins - metabolism
C-Terminus
Cell body
Chains
Cilia
Cilia - metabolism
Clearing
Compacts
Computational fluid dynamics
Cryoelectron Microscopy
Cytoplasm
Cytoplasm - metabolism
Domains
Dynein
Electron microscopy
Eukaryotes
Flagella
Gene Knockdown Techniques
Generators
Histones
Homology
Image Processing, Computer-Assisted
Inhibition
Mass spectrometry
Mass spectroscopy
Microscopy
Microtubules
Microtubules - physiology
Models, Molecular
Molecular motors
Motor activity
Movement
Mucus
Organelles
Primary ciliary dyskinesia
Protein Binding
Protein Conformation
Protein Domains
Protozoa
Protozoan Proteins - chemistry
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
Regulators
Respiratory diseases
Swimming
Synthesis
Tails
Tetrahymena
Tetrahymena thermophila - genetics
Tetrahymena thermophila - physiology
Triphosphatase
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Summary: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 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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.abe0526