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Structure of the Decorated Ciliary Doublet Microtubule
The axoneme of motile cilia is the largest macromolecular machine of eukaryotic cells. In humans, impaired axoneme function causes a range of ciliopathies. Axoneme assembly, structure, and motility require a radially arranged set of doublet microtubules, each decorated in repeating patterns with non...
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Published in: | Cell 2019-10, Vol.179 (4), p.909-922.e12 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The axoneme of motile cilia is the largest macromolecular machine of eukaryotic cells. In humans, impaired axoneme function causes a range of ciliopathies. Axoneme assembly, structure, and motility require a radially arranged set of doublet microtubules, each decorated in repeating patterns with non-tubulin components. We use single-particle cryo-electron microscopy to visualize and build an atomic model of the repeating structure of a native axonemal doublet microtubule, which reveals the identities, positions, repeat lengths, and interactions of 38 associated proteins, including 33 microtubule inner proteins (MIPs). The structure demonstrates how these proteins establish the unique architecture of doublet microtubules, maintain coherent periodicities along the axoneme, and stabilize the microtubules against the repeated mechanical stress induced by ciliary motility. Our work elucidates the architectural principles that underpin the assembly of this large, repetitive eukaryotic structure and provides a molecular basis for understanding the etiology of human ciliopathies.
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•High-resolution cryo-EM structure of a native axonemal doublet microtubule•Atomic model for the 48-nm repeat structure includes 38 proteins•Coherent register between different periodicities via interconnected networks•Insights into diverse MIP functions and roles in ciliopathies
Visualizing axonemal microtubules and the proteins that decorate them, on the outside and inside, points to how the underlying periodic architecture supports cilia function. |
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ISSN: | 0092-8674 1097-4172 |
DOI: | 10.1016/j.cell.2019.09.030 |