ArticlePloS one2023
α-Tubulin acetylation at lysine 40 regulates dendritic arborization and larval locomotion by promoting microtubule stability in Drosophila.
Article in PloS one, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 6 citations in OpenAlex.
- SPACA9 and MNMIP1 bridge the seam of spermatid manchette microtubules.The EMBO journal · 2026Article
- NAALADL1 modulates cellular resistance to Tumor Treating Fields in colorectal cancer.NPJ precision oncology · 2026Article
- Bridging the gap: an emerging link between tubulinopathies and ciliopathies.NPJ genomic medicine · 2026Review
- Glia-to-glia serotonin signaling directs MMP-dependent infiltration for experience-dependent synapse pruning.PLoS biology · 2025Article
- Mutating different α-tubulin acetylation sites has distinct effects on axon terminal morphogenesis inbioRxiv : the preprint server for biology · 2025Article
- Spatial arrangement, polarity, and posttranslational modifications of the microtubule system in the Drosophila eye.Cell and tissue research · 2024Article
- The α-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases.Cellular and molecular life sciences : CMLS · 2024Review
- Knockdown of SIRT2 Rescues YARS-induced Charcot-Marie-Tooth Neuropathy in Drosophila.Neuroscience bulletin · 2024Article
- ARHGEF5 binds Drebrin and affects α-tubulin acetylation to direct neuronal morphogenesis and migration during mouse brain development.Frontiers in molecular neuroscience · 2024Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Posttranslational modification of tubulin increases the dynamic complexity and functional diversity of microtubules. Acetylation of α-tubulin at Lys-40 is a highly conserved posttranslational modification that has been shown to improve the flexibility and resilience of microtubules. Here we studied the in vivo functions of α-tubulin acetylation by knocking-out Atat, the Drosophila α-tubulin acetyltransferase, and by mutating Lys-40 to Arg in α1-tubulin. We found a reduction in the dendritic arborization of larval class I dendritic arborization (da) neurons in both mutants. The dendritic developmental defects in atat mutants could be reversed by enhancing the stability of microtubules either through knocking down the microtubule severing protein Katanin 60 or through overexpressing tubulin-specific chaperone E, suggesting that α-tubulin deacetylation impairsed dendritic morphology by decreasing the stability of microtubules. Using time-lapse recordings, we found that atat and α1-tubulinK40R mutations dramatically increased the number of dendritic protrusions that were likely to be immature dendritic precursors. Finally, we showed that both Atat and α-tubulin acetylation were required in class I da neurons to control larval locomotion. These findings add novel insight into the current knowledge of the role of α-tubulin acetylation in regulating neuronal development and functions.
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