Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism
© 2023. Springer Nature Limited..
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.
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Medienart: |
E-Artikel |
Erscheinungsjahr: |
2023 |
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Erschienen: |
2023 |
Enthalten in: |
Zur Gesamtaufnahme - volume:14 |
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Enthalten in: |
Nature communications - 14(2023), 1 vom: 15. Sept., Seite 5741 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Ghanaeian, Avrin [VerfasserIn] |
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Links: |
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Themen: |
Amyloidogenic Proteins |
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Anmerkungen: |
Date Completed 18.09.2023 Date Revised 02.12.2023 published: Electronic UpdateOf: bioRxiv. 2023 Jun 01;:. - PMID 37398254 Citation Status MEDLINE |
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doi: |
10.1038/s41467-023-41480-7 |
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funding: |
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PPN (Katalog-ID): |
NLM362119716 |
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520 | |a 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 | ||
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700 | 1 | |a Bui, Khanh Huy |e verfasserin |4 aut | |
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