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Abstract
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 requires 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. Visualizing
axonemal microtubules and the proteins that decorate them, on the outside and inside,
points to how the underlying periodic architecture supports cilia function.