The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications
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Open Access
- 17 January 2020
- journal article
- research article
- Published by eLife Sciences Publications, Ltd in eLife
Abstract
Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the alpha- and beta-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.Funding Information
- Canadian Institutes of Health Research (PJT-156354)
- Natural Sciences and Engineering Research Council of Canada (RGPIN-2016-04954)
- Natural Sciences and Engineering Research Council of Canada (RGPIN-2018-04813)
- Canadian Institute for Advanced Research (Arzieli Global Scholar Program)
- Japan Society for the Promotion of Science
- Abdulla Al Ghurair Foundation for Education (Al Ghurair STEM program scholarship)
- Canada Research Chairs (950-229792)
- Natural Sciences and Engineering Research Council of Canada (RGPIN-2017-04649)
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