EMD-41270
Focused refinement of the N-DRC from the Tetrahymena WT subtomo
EMD-41270
Subtomogram averaging21.2 Å
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Map released: 20/09/2023
Last modified: 03/04/2024
Sample Organism:
Tetrahymena thermophila
Sample: Focused refinement of the N-DRC from the Tetrahymena WT subtomo
Deposition Authors: Ghanaeian AG, Majhi SM, McCaffrey CM, Nami BN, Black CB, Yang SK
,
Legal TL,
Papoulas OP,
Janowska MJ,
Valente-Paterno MV,
Marcotte EM
,
Wloga DW,
Bui KH
Sample: Focused refinement of the N-DRC from the Tetrahymena WT subtomo
Deposition Authors: Ghanaeian AG, Majhi SM, McCaffrey CM, Nami BN, Black CB, Yang SK
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Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism.
Ghanaeian A
,
Majhi S
,
McCafferty CL
,
Nami B
,
Black CS
,
Yang SK
,
Legal T
,
Papoulas O
,
Janowska M,
Valente-Paterno M,
Marcotte EM
,
Wloga D,
Bui KH
(2023) Nat Commun , 14 , 5741 - 5741
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(2023) Nat Commun , 14 , 5741 - 5741
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.
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.