Integrated modeling of the Nexin-dynein regulatory complex reveals its regulatory mechanism
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, utilizing cryo-electron microscopy in conjunction with biochemical cross-linking and integrative modeling, we localized 12 DRC subunits in the N-DRC structure of Tetrahymena thermophila . We also found that the CCDC96/113 complex is in close contact with the N-DRC. In addition, we revealed 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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UpdateIn: Nat Commun. 2023 Sep 15;14(1):5741. - PMID 37714832 |
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| Medienart: |
E-Artikel |
| Erscheinungsjahr: |
2023 |
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| Erschienen: |
2023 |
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Zur Gesamtaufnahme - year:2023 |
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| Enthalten in: |
bioRxiv : the preprint server for biology - (2023) vom: 01. Juni |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ghanaeian, Avrin [VerfasserIn] |
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Date Revised 22.09.2023 published: Electronic UpdateIn: Nat Commun. 2023 Sep 15;14(1):5741. - PMID 37714832 Citation Status PubMed-not-MEDLINE |
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| doi: |
10.1101/2023.05.31.543107 |
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NLM358994586 |
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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, utilizing cryo-electron microscopy in conjunction with biochemical cross-linking and integrative modeling, we localized 12 DRC subunits in the N-DRC structure of Tetrahymena thermophila . We also found that the CCDC96/113 complex is in close contact with the N-DRC. In addition, we revealed 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 McCaffrey, Caitie L |e verfasserin |4 aut | |
| 700 | 1 | |a Nami, Babak |e verfasserin |4 aut | |
| 700 | 1 | |a Black, Corbin S |e verfasserin |4 aut | |
| 700 | 1 | |a Yang, Shun Kai |e verfasserin |4 aut | |
| 700 | 1 | |a Legal, Thibault |e verfasserin |4 aut | |
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| 700 | 1 | |a Janowska, Martyna |e verfasserin |4 aut | |
| 700 | 1 | |a Valente-Paterno, Melissa |e verfasserin |4 aut | |
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