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-Structure paper
| Title | Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets. |
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| Journal, issue, pages | Nat Commun, Vol. 16, Issue 1, Page 1055, Year 2025 |
| Publish date | Jan 26, 2025 |
Authors | Aditya Chhatre / Ludek Stepanek / Adrian Pascal Nievergelt / Gonzalo Alvarez Viar / Stefan Diez / Gaia Pigino / ![]() |
| PubMed Abstract | Cilia assembly and function rely on the bidirectional transport of components between the cell body and ciliary tip via Intraflagellar Transport (IFT) trains. Anterograde and retrograde IFT trains ...Cilia assembly and function rely on the bidirectional transport of components between the cell body and ciliary tip via Intraflagellar Transport (IFT) trains. Anterograde and retrograde IFT trains travel along the B- and A-tubules of microtubule doublets, respectively, ensuring smooth traffic flow. However, the mechanism underlying this segregation remains unclear. Here, we test whether tubulin detyrosination (enriched on B-tubules) and tyrosination (enriched on A-tubules) have a role in IFT logistics. We report that knockout of tubulin detyrosinase VashL in Chlamydomonas reinhardtii causes frequent IFT train stoppages and impaired ciliary growth. By reconstituting IFT train motility on de-membranated axonemes and synthetic microtubules, we show that anterograde and retrograde trains preferentially associate with detyrosinated and tyrosinated microtubules, respectively. We propose that tubulin tyrosination/detyrosination is crucial for spatial segregation and collision-free IFT train motion, highlighting the significance of the tubulin code in ciliary transport. |
External links | Nat Commun / PubMed:39865093 / PubMed Central |
| Methods | EM (subtomogram averaging) |
| Resolution | 22.56 Å |
| Structure data | ![]() EMDB-52022: 96nm axonemal repeat of Chlamydomonas r. mutant IFT46-mNG VASHko lacking tubulin detyrosination |
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