The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications
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Abstract
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.
Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.
The record
- Venue
- eLife
- Topic
- Protist diversity and phylogeny
- Field
- Biochemistry, Genetics and Molecular Biology
- Canadian institutions
- McGill University
- Funders
- Japan Society for the Promotion of ScienceCanadian Institutes of Health ResearchNatural Sciences and Engineering Research Council of CanadaCanada Research ChairsCanadian Institute for Advanced Research
- Keywords
- MicrotubuleTetrahymenaCiliumTubulinCell biologyChlamydomonas reinhardtiiCytoskeletonChlamydomonasMicrotubule nucleationMotile ciliumChemistryBiologyBiophysicsCentrosomeCellBiochemistry
- Has abstract in OpenAlex
- yes