ArticleEMBO reports2017
Molecular interactions between tubulin tails and glutamylases reveal determinants of glutamylation patterns.
Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Structural Basis of Human Kinetochore-Microtubule Coupling by the Ndc80 and Ska Complexes.bioRxiv : the preprint server for biology · 2026Article
- Identification of a component of the tubulin poly-glutamylase complex required for phosphoinositide homeostasis and cilium assembly and maintenance.Nature communications · 2026Article
- Mechanistic insights into TTLL11 polyglutamylase-mediated primary tubulin chain elongation.Science advances · 2025Article
- The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylation.bioRxiv : the preprint server for biology · 2025Article
- CFAP100 couples microtubule glutamylation to spindle pole integrity in keratinocytes to promote epidermal development.Nature communications · 2025Article
- Carboxy-terminal polyglutamylation regulates signaling and phase separation of the Dishevelled protein.The EMBO journal · 2024Article
- Towards a Long-Read Sequencing Approach for the Molecular Diagnosis of RPGRInternational journal of molecular sciences · 2023Article
- Article
- Polyglutamylation: biology and analysis.Amino acids · 2022Review
- Post-translational polymodification of β1-tubulin regulates motor protein localisation in platelet production and function.Haematologica · 2022Article
- Reciprocal regulation of cellular mechanics and metabolism.Nature metabolism · 2021Review
- Tubulin post-translational modifications control neuronal development and functions.Developmental neurobiology · 2021Review
- The Emerging Roles of Axonemal Glutamylation in Regulation of Cilia Architecture and Functions.Frontiers in cell and developmental biology · 2021Review
- Structural basis for polyglutamate chain initiation and elongation by TTLL family enzymes.Nature structural & molecular biology · 2020Article
- The tubulin code and its role in controlling microtubule properties and functions.Nature reviews. Molecular cell biology · 2020Review
- Tubulin tails and their modifications regulate protein diffusion on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- RPGR gene therapy presents challenges in cloning the coding sequence.Expert opinion on biological therapy · 2020Review
- Molecular Strategies for RPGR Gene Therapy.Genes · 2019Review
- Axoneme polyglutamylation regulated by Joubert syndrome protein ARL13B controls ciliary targeting of signaling molecules.Nature communications · 2018Article
- Gene therapy for the treatment of X-linked retinitis pigmentosa.Expert opinion on orphan drugs · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Posttranslational modifications of tubulin currently emerge as key regulators of microtubule functions. Polyglutamylation generates a variety of modification patterns that are essential for controlling microtubule functions in different cell types and organelles, and deregulation of these patterns has been linked to ciliopathies, cancer and neurodegeneration. How the different glutamylating enzymes determine precise modification patterns has so far remained elusive. Using computational modelling, molecular dynamics simulations and mutational analyses we now show how the carboxy-terminal tails of tubulin bind into the active sites of glutamylases. Our models suggest that the glutamylation sites on α- and β-tubulins are determined by the positioning of the tails within the catalytic pocket. Moreover, we found that the binding modes of α- and β-tubulin tails are highly similar, implying that most enzymes could potentially modify both, α- and β-tubulin. This supports a model in which the binding of the enzymes to the entire microtubule lattice, but not the specificity of the C-terminal tubulin tails to their active sites, determines the catalytic specificities of glutamylases.
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