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Microtubules are cytoskeletal structures involved in stability, transport
and organization in the cell. The building blocks, the α- and β-tubulin
heterodimers, form protofilaments that associate laterally into the hollow
microtubule. Microtubule also exists as highly stable doublet microtubules
in the cilia where stability is needed for ciliary beating and function.
The doublet microtubule maintains its stability through interactions at
its inner and outer junctions where its A- and B-tubules meet. Here, using
cryo-electron microscopy, bioinformatics and mass spectrometry of the
doublets of Chlamydomonas reinhardtii and Tetrahymena thermophila, we
identified two new inner junction proteins, FAP276 and FAP106, and an
inner junction-associated protein, FAP126, thus presenting the complete
answer to the inner junction identity and localization. Our structural
study of the doublets shows that the inner junction serves as an
interaction hub that involves tubulin post-translational modifications.
These interactions contribute to the stability of the doublet and hence,
normal ciliary motility.
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