Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets
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 travel along the B- and A-tubules of microtubule doublets, respectively, ensuring smooth traff...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-01-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-56098-0 |
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| author | Aditya Chhatre Ludek Stepanek Adrian Pascal Nievergelt Gonzalo Alvarez Viar Stefan Diez Gaia Pigino |
| author_facet | Aditya Chhatre Ludek Stepanek Adrian Pascal Nievergelt Gonzalo Alvarez Viar Stefan Diez Gaia Pigino |
| author_sort | Aditya Chhatre |
| collection | DOAJ |
| description | 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 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. |
| format | Article |
| id | doaj-art-7d473309ee3441d2a3bb4ac1f7ee81df |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-7d473309ee3441d2a3bb4ac1f7ee81df2025-01-26T12:41:50ZengNature PortfolioNature Communications2041-17232025-01-0116111310.1038/s41467-025-56098-0Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doubletsAditya Chhatre0Ludek Stepanek1Adrian Pascal Nievergelt2Gonzalo Alvarez Viar3Stefan Diez4Gaia Pigino5Cluster of Excellence Physics of Life, TUD Dresden University of TechnologyMax Planck Institute of Molecular Cell Biology and GeneticsMax Planck Institute of Molecular Cell Biology and GeneticsHuman TechnopoleCluster of Excellence Physics of Life, TUD Dresden University of TechnologyCluster of Excellence Physics of Life, TUD Dresden University of TechnologyAbstract 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.https://doi.org/10.1038/s41467-025-56098-0 |
| spellingShingle | Aditya Chhatre Ludek Stepanek Adrian Pascal Nievergelt Gonzalo Alvarez Viar Stefan Diez Gaia Pigino Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets Nature Communications |
| title | Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets |
| title_full | Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets |
| title_fullStr | Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets |
| title_full_unstemmed | Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets |
| title_short | Tubulin tyrosination/detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets |
| title_sort | tubulin tyrosination detyrosination regulate the affinity and sorting of intraflagellar transport trains on axonemal microtubule doublets |
| url | https://doi.org/10.1038/s41467-025-56098-0 |
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