ArticleProceedings of the National Academy of Sciences of the United States of America2017
Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 35 citations in OpenAlex.
- 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
- Two anchoring proteins control daughter apical complex assembly inbioRxiv : the preprint server for biology · 2026Article
- The tubulin code in acute ischemic stroke: post-translational reprogramming of the neuronal cytoskeleton and implications for phase-specific neuroprotection.Frontiers in neuroscience · 2026Review
- The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylation.bioRxiv : the preprint server for biology · 2025Article
- Structural basis for α-tubulin-specific and modification state-dependent glutamylation.Nature chemical biology · 2024Article
- Protofilament-specific nanopatterns of tubulin post-translational modifications regulate the mechanics of ciliary beating.Current biology : CB · 2024Article
- Article
- Tubulin glycylation controls ciliary motility through modulation of outer-arm dyneins.Molecular biology of the cell · 2024Article
- Regulatory mechanisms of the dynein-2 motility by post-translational modification revealed by MD simulation.Scientific reports · 2023Article
- Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing.Developmental cell · 2022Article
- Reconstituting Microtubules: A Decades-Long Effort From Building Block Identification to the Generation of Recombinant α/β-Tubulin.Frontiers in cell and developmental biology · 2022Review
- 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 in Microtubule Dynamics and Information Encoding.Developmental cell · 2020Review
- Pby1 is a direct partner of the Dcp2 decapping enzyme.Nucleic acids research · 2020Article
- Frequent mutation of hypoxia-related genes in persistent pulmonary hypertension of the newborn.Respiratory research · 2020Article
- Article
- How cells exploit tubulin diversity to build functional cellular microtubule mosaics.Current opinion in cell biology · 2019Review
- The tubulin code in neuronal polarity.Current opinion in neurobiology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Glycylation and glutamylation, the posttranslational addition of glycines and glutamates to genetically encoded glutamates in the intrinsically disordered tubulin C-terminal tails, are crucial for the biogenesis and stability of cilia and flagella and play important roles in metazoan development. Members of the diverse family of tubulin tyrosine ligase-like (TTLL) enzymes catalyze these modifications, which are part of an evolutionarily conserved and complex tubulin code that regulates microtubule interactions with cellular effectors. The site specificity of TTLL enzymes and their biochemical interplay remain largely unknown. Here, we report an in vitro characterization of a tubulin glycylase. We show that TTLL3 glycylates the β-tubulin tail at four sites in a hierarchical order and that TTLL3 and the glutamylase TTLL7 compete for overlapping sites on the tubulin tail, providing a molecular basis for the anticorrelation between glutamylation and glycylation observed in axonemes. This anticorrelation demonstrates how a combinatorial tubulin code written in two different posttranslational modifications can arise through the activities of related but distinct TTLL enzymes. To elucidate what structural elements differentiate TTLL glycylases from glutamylases, with which they share the common TTL scaffold, we determined the TTLL3 X-ray structure at 2.3-Å resolution. This structure reveals two architectural elements unique to glycyl initiases and critical for their activity. Thus, our work sheds light on the structural and functional diversification of TTLL enzymes, and constitutes an initial important step toward understanding how the tubulin code is written through the intersection of activities of multiple TTLL enzymes.
Indexed as
Identifiers
What OpenQuestion holds
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.