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 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...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2021-02, Vol.371 (6532), p.910-916
Hauptverfasser:	Mali, Girish R., Ali, Ferdos Abid, Lau, Clinton K., Begum, Farida, Boulanger, Jerome, Howe, Jonathan D., Chen, Zhuo A., Rappsilber, Juri, Skehel, Mark, Carter, Andrew P.
Format:	Artikel
Sprache:	eng
Schlagworte:	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 Multidisciplinary Sciences Organelles Primary ciliary dyskinesia Protein Binding Protein Conformation Protein Domains Protozoa Protozoan Proteins - chemistry Protozoan Proteins - genetics Protozoan Proteins - metabolism Regulators Respiratory diseases Science & Technology Science & Technology - Other Topics Swimming Synthesis Tails Tetrahymena Tetrahymena thermophila - genetics Tetrahymena thermophila - physiology Triphosphatase
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Beschreibung
Zusammenfassung:	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.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.abe0526