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

Author:

Ghanaeian AvrinORCID,Majhi SumitaORCID,McCafferty Caitlyn L.,Nami BabakORCID,Black Corbin S.ORCID,Yang Shun KaiORCID,Legal ThibaultORCID,Papoulas OpheliaORCID,Janowska Martyna,Valente-Paterno Melissa,Marcotte Edward M.ORCID,Wloga Dorota,Bui Khanh HuyORCID

Abstract

AbstractCilia 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.

Funder

Gouvernement du Canada | Canadian Institutes of Health Research

Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada

Welch Foundation

U.S. Department of Health & Human Services | National Institutes of Health

Narodowe Centrum Nauki

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry,Multidisciplinary

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