The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation
Open accessAbstract
Long-lived microtubules found in ciliary axonemes, neuronal processes, and migrating cells are marked by α-tubulin acetylation on lysine 40, a modification that takes place inside the microtubule lumen. The physiological importance of microtubule acetylation remains elusive. Here, we identify a BBSome-associated protein that we name αTAT1, with a highly specific α - t ubulin K40 a cetyl t ransferase activity and a catalytic preference for microtubules over free tubulin. In mammalian cells, the catalytic activity of αTAT1 is necessary and sufficient for α-tubulin K40 acetylation. Remarkably, αTAT1 is universally and exclusively conserved in ciliated organisms, and is required for the acetylation of axonemal microtubules and for the normal kinetics of primary cilium assembly. In Caenorhabditis elegans , microtubule acetylation is most prominent in touch receptor neurons (TRNs) and MEC-17, a homolog of αTAT1, and its paralog αTAT-2 are required for α-tubulin acetylation and for two distinct types of touch sensation. Furthermore, in animals lacking MEC-17, αTAT-2, and the sole C. elegans K40α-tubulin MEC-12, touch sensation can be restored by expression of an acetyl-mimic MEC-12[K40Q]. We conclude that αTAT1 is the major and possibly the sole α-tubulin K40 acetyltransferase in mammals and nematodes, and that tubulin acetylation plays a conserved role in several microtubule-based processes.
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Cites
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Cited by
The tubulin code and its role in controlling microtubule properties and functions
Janke, C., & Magiera, M. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0214-3 · Cited by 956
Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions
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The tubulin code: Molecular components, readout mechanisms, and functions
Janke, C. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201406055 · Cited by 532
Establishing and regulating the composition of cilia for signal transduction
Nachury, M. V., & Mick, D. U. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0116-4 · Cited by 397
Self-citationCauses and Consequences of Microtubule Acetylation
Janke, C., & Montagnac, G. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.044 · Cited by 312
Metadata
- Authors
- Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B., & Nachury, M. V.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-11-10
- Volume
- 107
- Issue
- 50
- Pages
- 21517-21522
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1984167248
- Cited by
- 472
- References
- 42
- FWCI
- 13.41
- Type
- journal article
- Language
- en
- Open access
- green
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- Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B., & Nachury, M. V. (2010). The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1013728107
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