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| Title | Protofilament-specific nanopatterns of tubulin post-translational modifications regulate the mechanics of ciliary beating. |
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| Journal, issue, pages | Curr Biol, Year 2024 |
| Publish date | Sep 12, 2024 |
 Authors | Gonzalo Alvarez Viar / Nikolai Klena / Fabrizio Martino / Adrian Pascal Nievergelt / Davide Bolognini / Paola Capasso / Gaia Pigino /   |
| PubMed Abstract | Controlling ciliary beating is essential for motility and signaling in eukaryotes. This process relies on the regulation of various axonemal proteins that assemble in stereotyped patterns onto ...Controlling ciliary beating is essential for motility and signaling in eukaryotes. This process relies on the regulation of various axonemal proteins that assemble in stereotyped patterns onto individual microtubules of the ciliary structure. Additionally, each axonemal protein interacts exclusively with determined tubulin protofilaments of the neighboring microtubule to carry out its function. While it is known that tubulin post-translational modifications (PTMs) are important for proper ciliary motility, the mode and extent to which they contribute to these interactions remain poorly understood. Currently, the prevailing understanding is that PTMs can confer functional specialization at the level of individual microtubules. However, this paradigm falls short of explaining how the tubulin code can manage the complexity of the axonemal structure where functional interactions happen in defined patterns at the sub-microtubular scale. Here, we combine immuno-cryo-electron tomography (cryo-ET), expansion microscopy, and mutant analysis to show that, in motile cilia, tubulin glycylation and polyglutamylation form mutually exclusive protofilament-specific nanopatterns at a sub-microtubular scale. These nanopatterns are consistent with the distributions of axonemal dyneins and nexin-dynein regulatory complexes, respectively, and are indispensable for their regulation during ciliary beating. Our findings offer a new paradigm for understanding how different tubulin PTMs, such as glycylation, glutamylation, acetylation, tyrosination, and detyrosination, can coexist within the ciliary structure and specialize individual protofilaments for the regulation of diverse protein complexes. The identification of a ciliary tubulin nanocode by cryo-ET suggests the need for high-resolution studies to better understand the molecular role of PTMs in other cellular compartments beyond the cilium. |
 External links | Curr Biol / PubMed:39270640 |
| Methods | EM (subtomogram averaging) |
| Resolution | 12.08 - 35.0 Å |
| Structure data |  EMDB-50495: Axonemal doublet 48nm repeat of the tubulin glycylation deficient C. reinhardtii strain ttll3::BSD  EMDB-50501: 48nm repeat of the axonemal doublets of the tubulin polyglutamylation deficient C. reinhardtii strain ttll9::KO  EMDB-50505: 32nm repeat of the central pair complex 1 of the tubulin glycylation depleted C.reinhardtii strain ttll3::BSD  EMDB-50513: 32nm repeat of the central pair complex 1 of the tubulin polyglutamylation deficient C.reinhardtii strain ttll9::NAT  EMDB-50559: 16nm repeat of the central pair complex 2 of the tubulin glycylation depleted strain ttll3::BSD of C.reinhardtii  EMDB-50560: 16nm repeat of the central pair complex 2 of the tubulin polyglutamylation deficient ttll9::NAT strain from C.reinhardtii  EMDB-50561: 96nm repeat of the C.reinhardtii axoneme  EMDB-50563: 96nm repeat of the axonemal doublet from mouse respiratory cilia  EMDB-50564: 96 nm repeat of the axonemal microtubule doublets of the tpg1 strain from C.reinhardtii  EMDB-50565: 96nm repeat of the axonemal doublets from the tubulin glycylation depleted ttll3 strain from C.reinhardtii  EMDB-50568: 96nm repeat of the axonemal doublets from C.reinhardtii decorated with polyE antibodies  EMDB-50569: 96nm repeat of the axonemal doublets of the tpg1 strain from C.reinhardtii incubated with polyE antiobodies  EMDB-50572: 96nm repeat of the axonemal doublets of the ida5 strain from C.reinhardtii decorated with polyE antibodies  EMDB-50573: 96nm repeat of the axonemal doublets of mouse respiratory cilia decorated with polyE antibodies  EMDB-50575: 96nm repeat of the axonemal doublets of C.reinhardtii decorated with Glypep1 antibodies  EMDB-50577: 96nm repeat of the axonemal doublets of mouse respiratory cilia incubated with Glypep1 antibodies  EMDB-50579: 96nm repeat of the axonemal doublet of reactivated axonemes of C.reinhardtii  EMDB-50596: 96nm repeat of the axonemal doublets from the ttll3 strain of C. reinhardtii incubated with Glypep1 antibodies  EMDB-50597: 96nm repeat of the axonemal doublets of the ida5 strain from C.reinhardtii decoreated with Glypep1 antibodies |
| Source |
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C.reinhardtii (plant)
M.musculus (house mouse)