ArticleNature structural & molecular biology2019
Structural basis of tubulin detyrosination by vasohibins.
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 41 papers.
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Who cites it
41 citing papers in PubMed, 40 citations in OpenAlex.
- Towards a systems-level view of the microtubule cytoskeleton and its functions in physiology and disease.Nature reviews. Molecular cell biology · 2026Review
- Prognostic, diagnostic and therapeutic value of the cancer tubulin code.Cancer metastasis reviews · 2026Review
- The molecular mechanisms of the ShosTA system in mediating anti-phage defense.Nucleic acids research · 2026Article
- Tubulin Post-Translational Modifications in Cardiovascular Diseases: Emerging Mechanisms and Therapeutic Modulation by Traditional Chinese Medicine.Drug design, development and therapy · 2026Review
- KY216-tubulin complex captures VASH2 to inhibit NSCLC metastasis.Nature communications · 2025Article
- Suppressing microtubule detyrosination augments adeno-associated virus 2 endosomal escape and gene delivery.Journal of cell science · 2025Article
- Cnicin: a promising drug for promoting nerve repair.Frontiers in cell and developmental biology · 2025Article
- Molecular Basis of VCPIP1 and P97/VCP Interaction Reveals Its Functions in Post-Mitotic Golgi Reassembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- 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
- Microtubule-associated protein MAP7 promotes tubulin posttranslational modifications and cargo transport to enable osmotic adaptation.Developmental cell · 2024Article
- Targeting Vasohibins to Promote Axon Regeneration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Revealing the inhibitory effect of VASH1 on ovarian cancer from multiple perspectives.Cancer biology & therapy · 2023Article
- 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
- Macromolecular Crowding Tailors the Microtubule Cytoskeleton Through Tubulin Modifications and Microtubule-Associated Proteins.bioRxiv : the preprint server for biology · 2023Article
- Mechanistic Analysis of CCP1 in Generating ΔC2 α-Tubulin in Mammalian Cells and Photoreceptor Neurons.Biomolecules · 2023Article
- VASH1-SVBP and VASH2-SVBP generate different detyrosination profiles on microtubules.The Journal of cell biology · 2023Article
- Role of tubulin post-translational modifications in peripheral neuropathy.Experimental neurology · 2023Review
- Tension of plus-end tracking protein Clip170 confers directionality and aggressiveness during breast cancer migration.Cell death & disease · 2022Article
- [Vasohibin-2 promotes proliferation and metastasis of cervical cancer cells by regulating epithelial-mesenchymal transition].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Microtubules are regulated by post-translational modifications of tubulin. The ligation and cleavage of the carboxy-terminal tyrosine of α-tubulin impact microtubule functions during mitosis, cardiomyocyte contraction and neuronal processes. Tubulin tyrosination and detyrosination are mediated by tubulin tyrosine ligase and the recently discovered tubulin detyrosinases, vasohibin 1 and 2 (VASH1 and VASH2) bound to the small vasohibin-binding protein (SVBP). Here, we report the crystal structures of human VASH1-SVBP alone, in complex with a tyrosine-derived covalent inhibitor and bound to the natural product parthenolide. The structures and subsequent mutagenesis analyses explain the requirement for SVBP during tubulin detyrosination, and reveal the basis for the recognition of the C-terminal tyrosine and the acidic α-tubulin tail by VASH1. The VASH1-SVBP-parthenolide structure provides a framework for designing more effective chemical inhibitors of vasohibins, which can be valuable for dissecting their biological functions and may have therapeutic potential.
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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.