ArticleEukaryotic cell2008
Glutamylation on alpha-tubulin is not essential but affects the assembly and functions of a subset of microtubules in Tetrahymena thermophila.
Article in Eukaryotic cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 104 citations in OpenAlex.
- Prognostic, diagnostic and therapeutic value of the cancer tubulin code.Cancer metastasis reviews · 2026Review
- Tubulin glutamylation: a key regulator of flagella, cilia, centrosomes, and disease pathways.Journal of biomedical science · 2026Review
- Tubulin hyperglutamylation induces retinal degeneration by disrupting ciliary architecture and protein trafficking.Zoological research · 2026Article
- Emerging Roles of Tubulin Isoforms and Their Post-Translational Modifications in Microtubule-Based Transport and Cellular Functions.Biomolecules · 2026Review
- Tubulin monoglutamylation is sufficient to rescue the ciliary motility defects in aFrontiers in cell and developmental biology · 2026Article
- Heterogeneity of radial spoke components in Tetrahymena cilia.Cellular and molecular life sciences : CMLS · 2025Article
- Mouse radial spoke 3 is a metabolic and regulatory hub in cilia.Nature structural & molecular biology · 2025Article
- The function of the ATG8 in the cilia and cortical microtubule maintenance of Euplotes amieti.Protoplasma · 2024Article
- Article
- The tubulin database: Linking mutations, modifications, ligands and local interactions.PloS one · 2023Article
- Cfap91-Dependent Stability of the RS2 and RS3 Base Proteins and Adjacent Inner Dynein Arms inCells · 2022Article
- Ciliate Microtubule Diversities: Insights from the EFBTU3 Tubulin in the Antarctic CiliateMicroorganisms · 2022Article
- Ciliate cortical organization and dynamics for cell motility: Comparing ciliates and vertebrates.The Journal of eukaryotic microbiology · 2022Review
- Molecular Evolution of Tubulins in Diatoms.International journal of molecular sciences · 2022Article
- Microtubules in Microorganisms: How Tubulin Isotypes Contribute to Diverse Cytoskeletal Functions.Frontiers in cell and developmental biology · 2022Review
- The macronuclear genome of the Antarctic psychrophilic marine ciliate Euplotes focardii reveals new insights on molecular cold adaptation.Scientific reports · 2021Article
- Composition and function of the C1b/C1f region in the ciliary central apparatus.Scientific reports · 2021Article
- Ccdc113/Ccdc96 complex, a novel regulator of ciliary beating that connects radial spoke 3 to dynein g and the nexin link.PLoS genetics · 2021Article
- The Emerging Roles of Axonemal Glutamylation in Regulation of Cilia Architecture and Functions.Frontiers in cell and developmental biology · 2021Review
- C-Terminal Tail Polyglycylation and Polyglutamylation Alter Microtubule Mechanical Properties.Biophysical journal · 2020Article
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Authors and funding
13 authors at 9 institutions in 3 countries.
Funding
Abstract
Tubulin undergoes glutamylation, a conserved posttranslational modification of poorly understood function. We show here that in the ciliate Tetrahymena, most of the microtubule arrays contain glutamylated tubulin. However, the length of the polyglutamyl side chain is spatially regulated, with the longest side chains present on ciliary and basal body microtubules. We focused our efforts on the function of glutamylation on the alpha-tubulin subunit. By site-directed mutagenesis, we show that all six glutamates of the C-terminal tail domain of alpha-tubulin that provide potential sites for glutamylation are not essential but are needed for normal rates of cell multiplication and cilium-based functions (phagocytosis and cell motility). By comparative phylogeny and biochemical assays, we identify two conserved tubulin tyrosine ligase (TTL) domain proteins, Ttll1p and Ttll9p, as alpha-tubulin-preferring glutamyl ligase enzymes. In an in vitro microtubule glutamylation assay, Ttll1p showed a chain-initiating activity while Ttll9p had primarily a chain-elongating activity. GFP-Ttll1p localized mainly to basal bodies, while GFP-Ttll9p localized to cilia. Disruption of the TTLL1 and TTLL9 genes decreased the rates of cell multiplication and phagocytosis. Cells lacking both genes had fewer cortical microtubules and showed defects in the maturation of basal bodies. We conclude that glutamylation on alpha-tubulin is not essential but is required for efficiency of assembly and function of a subset of microtubule-based organelles. Furthermore, the spatial restriction of modifying enzymes appears to be a major mechanism that drives differential glutamylation at the subcellular level.
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