αTAT1 is the major α-tubulin acetyltransferase in mice
Open accessAbstract
Post-translational modification of tubulin serves as a powerful means for rapidly adjusting the functional diversity of microtubules. Acetylation of the ε-amino group of K40 in α-tubulin is one such modification that is highly conserved in ciliated organisms. Recently, αTAT1, a Gcn5-related N-acetyltransferase, was identified as an α-tubulin acetyltransferase in Tetrahymena and C. elegans. Here we generate mice with a targeted deletion of Atat1 to determine its function in mammals. Remarkably, we observe a loss of detectable K40 α-tubulin acetylation in these mice across multiple tissues and in cellular structures such as cilia and axons where acetylation is normally enriched. Mice are viable and develop normally, however, the absence of Atat1 impacts upon sperm motility and male mouse fertility, and increases microtubule stability. Thus, αTAT1 has a conserved function as the major α-tubulin acetyltransferase in ciliated organisms and has an important role in regulating subcellular specialization of subsets of microtubules.
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Depletion of αTAT1 did not decrease total RLC phosphorylation but increased its accumulation in the lamella, concomitant with impaired anteroposterior cell polarization.
“Interestingly, depletion of the tubulin acetyltransferase αTAT1 [22, 23] did not decrease total RLC phosphorylation but increased its accumulation in the lamella, concomitant with impaired anteroposterior cell polarization.”
αTAT1 depletion decreases K40 α-tubulin acetylation.
“Accordingly, αTAT1 depletion decreases K40 α‐tubulin acetylation [22, 23], which should increase retention of GEF‐H1 in microtubules.”
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- Authors
- Kalebic, N., Sorrentino, S., Perlas, E., Bolasco, G., Martinez, C., & Heppenstall, P. A.
- Affiliations
- European Molecular Biology Laboratory (IT)
- Corresponding author
- Heppenstall, Paul A.
- Venue
- Nature Communications
- Published
- 2013-06-10
- Volume
- 4
- Issue
- 1
- Pages
- 1962-1962
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2026231028
- Cited by
- 241
- References
- 7
- Citations by year
- 2026: 20 · 2025: 25 · 2024: 20 · 2023: 16 · 2022: 24 · 2021: 20 · 2020: 19 · 2019: 18 · 2018: 17 · 2017: 17 · 2016: 17 · 2015: 13 · 2014: 15
- FWCI
- 6.91
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Communications (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- SDL (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Cystic Fibrosis Research Advances
- Keywords
- alpha-tubulin acetylation, microtubule stability, cilia, axons, sperm motility, male fertility, GCN5-related N-acetyltransferase, tubulin post-translational modifications
- MeSH terms
- Acetylation, Acetyltransferases, Alleles, Animals, Fibroblasts, Lysine, Male, Microtubule Proteins, Microtubules, Phenotype, Spermatozoa, Testis, Tubulin, Nocodazole, Genome, Mice, Knockout, Protein Transport, Mice, Genetic Loci, Polymerization
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