Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism

Avrin Ghanaeian, Sumita Majhi, Caitlyn L. McCafferty, Babak Nami, Corbin S. Black, Shun Kai Yang, Thibault Legal, Ophelia Papoulas, Martyna Janowska, Melissa Valente-Paterno, Edward M. Marcotte, Dorota Wloga () and Khanh Huy Bui ()
Additional contact information
Avrin Ghanaeian: McGill University
Sumita Majhi: Nencki Institute of Experimental Biology of Polish Academy of Sciences
Caitlyn L. McCafferty: University of Texas
Babak Nami: Hospital for Sick Children
Corbin S. Black: McGill University
Shun Kai Yang: McGill University
Thibault Legal: McGill University
Ophelia Papoulas: University of Texas
Martyna Janowska: Nencki Institute of Experimental Biology of Polish Academy of Sciences
Melissa Valente-Paterno: McGill University
Edward M. Marcotte: University of Texas
Dorota Wloga: Nencki Institute of Experimental Biology of Polish Academy of Sciences
Khanh Huy Bui: McGill University

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: Abstract Cilia are hairlike protrusions that project from the surface of eukaryotic cells and play key roles in cell signaling and motility. Ciliary motility is regulated by the conserved nexin-dynein regulatory complex (N-DRC), which links adjacent doublet microtubules and regulates and coordinates the activity of outer doublet complexes. Despite its critical role in cilia motility, the assembly and molecular basis of the regulatory mechanism are poorly understood. Here, using cryo-electron microscopy in conjunction with biochemical cross-linking and integrative modeling, we localize 12 DRC subunits in the N-DRC structure of Tetrahymena thermophila. We also find that the CCDC96/113 complex is in close contact with the DRC9/10 in the linker region. In addition, we reveal that the N-DRC is associated with a network of coiled-coil proteins that most likely mediates N-DRC regulatory activity.

Date: 2023
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DOI: 10.1038/s41467-023-41480-7

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