ArticleNature structural & molecular biology2019
Structural basis of tubulin detyrosination by the vasohibin-SVBP enzyme complex.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 56 citations in OpenAlex.
- Brassinosteroids promote sugar synthesis by inhibiting BIN2 phosphorylation of phosphoenolpyruvate carboxykinase.Nature plants · 2026Article
- Condensation of MATCAP promotes CENP-E-dependent chromosome congression in mitosis.Nature communications · 2026Article
- Prognostic, diagnostic and therapeutic value of the cancer tubulin code.Cancer metastasis reviews · 2026Review
- Article
- An exploratory exome-wide machine learning analysis identifies candidate host gene signatures associated with Long COVID in a large admixed Brazilian cohort.Frontiers in medicine · 2026Article
- Tubulin Post-Translational Modifications in Cardiovascular Diseases: Emerging Mechanisms and Therapeutic Modulation by Traditional Chinese Medicine.Drug design, development and therapy · 2026Review
- From microtubule remodeling to clinical translation: the multifaceted roles of vasohibin-1 in disease modulation.Frontiers in immunology · 2026Review
- KY216-tubulin complex captures VASH2 to inhibit NSCLC metastasis.Nature communications · 2025Article
- Brassinosteroids promote sugar synthesis by inhibiting BIN2 phosphorylation of phosphoenolpyruvate carboxykinase.bioRxiv : the preprint server for biology · 2025Article
- Mechanistic insights into TTLL11 polyglutamylase-mediated primary tubulin chain elongation.Science advances · 2025Article
- Review
- VASH2 enhances KIF3C-mediated EGFR-endosomal recycling to promote aggression and chemoresistance of lung squamous cell carcinoma by increasing tubulin detyrosination.Cell death & disease · 2024Article
- Targeting Vasohibins to Promote Axon Regeneration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Structure-based virtual screening identifies small-molecule inhibitors of O-fucosyltransferase SPINDLY in Arabidopsis.The Plant cell · 2024Article
- Interplay between stochastic enzyme activity and microtubule stability drives detyrosination enrichment on microtubule subsets.Current biology : CB · 2023Article
- Tubulin engineering by semi-synthesis reveals that polyglutamylation directs detyrosination.Nature chemistry · 2023Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Post-translational modifications of tubulin: their role in cancers and the regulation of signaling molecules.Cancer gene therapy · 2023Review
- VASH1-SVBP and VASH2-SVBP generate different detyrosination profiles on microtubules.The Journal of cell biology · 2023Article
- Tubulin tyrosination regulates synaptic function and is disrupted in Alzheimer's disease.Brain : a journal of neurology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vasohibins are tubulin tyrosine carboxypeptidases that are important in neuron physiology. We examined the crystal structures of human vasohibin 1 and 2 in complex with small vasohibin-binding protein (SVBP) in the absence and presence of different inhibitors and a C-terminal α-tubulin peptide. In combination with functional data, we propose that SVBP acts as an activator of vasohibins. An extended groove and a distinctive surface residue patch of vasohibins define the specific determinants for recognizing and cleaving the C-terminal tyrosine of α-tubulin and for binding microtubules, respectively. The vasohibin-SVBP interaction and the ability of the enzyme complex to associate with microtubules regulate axon specification of neurons. Our results define the structural basis of tubulin detyrosination by vasohibins and show the relevance of this process for neuronal development. Our findings offer a unique platform for developing drugs against human conditions with abnormal tubulin tyrosination levels, such as cancer, heart defects and possibly brain disorders.
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.