ArticleProceedings of the National Academy of Sciences of the United States of America2016
Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 116 citations in OpenAlex.
- Protocol for systematic identification of microtubule luminal proteins using knock-in BioID proximity labeling and fluorescence imaging validation.STAR protocols · 2026Article
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Prognostic, diagnostic and therapeutic value of the cancer tubulin code.Cancer metastasis reviews · 2026Review
- Microtubule lattice conformation and integrity regulate α-tubulin acetylation.Communications biology · 2026Article
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- A genetically encoded microtubule bundler for causal dissection of microtubule bundling in cells.bioRxiv : the preprint server for biology · 2026Article
- Systematic identification of microtubule lumen proteins reveals a taxane-sensitive luminal resident JPT2 regulating MEC17 accessibility.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mutations in the β-tubulin TUBB impair ciliogenesis and are associated with ciliopathy-like phenotypes.Nature communications · 2025Article
- Microtubule acetylation is not required for HIV-1 infection or TRIM69-mediated restriction of HIV-1 infection.Journal of virology · 2025Article
- How does the tubulin code facilitate directed cell migration?Biochemical Society transactions · 2025Review
- Cryo-ET suggests tubulin chaperones form a subset of microtubule lumenal particles with a role in maintaining neuronal microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Tubulin acetyltransferases access and modify the microtubule luminal K40 residue through anchors in taxane-binding pockets.Nature structural & molecular biology · 2025Article
- Tubulin Acetylation Enhances Microtubule Stability in Trabecular Meshwork Cells Under Mechanical Stress.Investigative ophthalmology & visual science · 2025Article
- Acetylation and Deacetylation of Cytoskeleton-Associated Proteins.Results and problems in cell differentiation · 2025Review
- Microtubule shaft integrity emerges as a crucial determinant of the acetylation pattern.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Tubulin Acetylation: A Critical Regulator of Microtubule Function.Results and problems in cell differentiation · 2025Review
- Suppression of microtubule acetylation mediates the anti-leukemic effect of CDK9 inhibition.Cancer cell international · 2024Article
- The methylome of motile cilia.Molecular biology of the cell · 2024Article
- MFN2 coordinates mitochondria motility with α-tubulin acetylation and this regulation is disrupted in CMT2A.iScience · 2024Article
- The α-tubulin acetyltransferase ATAT1: structure, cellular functions, and its emerging role in human diseases.Cellular and molecular life sciences : CMLS · 2024Review
7 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Microtubules are structural polymers inside of cells that are subject to posttranslational modifications. These posttranslational modifications create functionally distinct subsets of microtubule networks in the cell, and acetylation is the only modification that takes place in the hollow lumen of the microtubule. Although it is known that the α-tubulin acetyltransferase (αTAT1) is the primary enzyme responsible for microtubule acetylation, the mechanism for how αTAT1 enters the microtubule lumen to access its acetylation sites is not well understood. By performing biochemical assays, fluorescence and electron microscopy experiments, and computational simulations, we found that αTAT1 enters the microtubule lumen through the microtubule ends, and through bends or breaks in the lattice. Thus, microtubule structure is an important determinant in the acetylation process. In addition, once αTAT1 enters the microtubule lumen, the mobility of αTAT1 within the lumen is controlled by the affinity of αTAT1 for its acetylation sites, due to the rapid rebinding of αTAT1 onto highly concentrated α-tubulin acetylation sites. These results have important implications for how acetylation could gradually accumulate on stable subsets of microtubules inside of the cell.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.