ArticleCurrent biology : CB2023
Microtubule detyrosination by VASH1/SVBP is regulated by the conformational state of tubulin in the lattice.
Article in Current biology : CB, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- A nine-gene diagnostic model for IgA nephropathy based on multi-cohort machine learning: integrating gene expression and immunohistochemical validation.Renal failure · 2026Article
- Paclitaxel induces NM2-dependent cellular contraction through GEF-H1 dissociation from microtubules and RhoA/ROCK activation in cancer cells.Molecular oncology · 2026Article
- Dissecting Structural and Functional Determinants of Microtubules Stabilization through Guided Chemical Modulation.Journal of medicinal chemistry · 2026Article
- Condensation of MATCAP promotes CENP-E-dependent chromosome congression in mitosis.Nature communications · 2026Article
- Microtubule lattice conformation and integrity regulate α-tubulin acetylation.Communications biology · 2026Article
- MATCAP1 preferentially binds an expanded tubulin conformation to generate detyrosinated and ΔC2 α-tubulin.The EMBO journal · 2026Article
- Optogenetic Tools for Spatiotemporal Interrogation of Cytoskeletal Dynamics.Bioconjugate chemistry · 2026Review
- Microtubules in the axon are GDP bound but adopt a stable GTP-like expanded state.Nature structural & molecular biology · 2026Article
- Article
- Peptide-based covalent inhibitor of tubulin detyrosination promotes mesenchymal-to-epithelial transition in lung cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation.bioRxiv : the preprint server for biology · 2025Article
- Microtubules and mechanosensing: key players in endothelial responses to mechanical stimuli.Cellular and molecular life sciences : CMLS · 2025Review
- Recombinant Monoclonal Antibodies for Detecting the Tubulin Post-Translational Modifications Glutamylation and Lysine-40 Acetylation.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Deep learning-based cytoskeleton segmentation for accurate high-throughput measurement of cytoskeleton density.Protoplasma · 2025Article
- Diverse microtubule-binding repeats regulate TPX2 activities at distinct locations within the spindle.The Journal of cell biology · 2025Article
- How does the tubulin code facilitate directed cell migration?Biochemical Society transactions · 2025Review
- Doublecortin restricts neuronal branching by regulating tubulin polyglutamylation.Nature communications · 2025Article
- StableMARK-decorated microtubules in cells have expanded lattices.The Journal of cell biology · 2025Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Tubulin, a heterodimer of α- and β-tubulin, is a GTPase that assembles into microtubule (MT) polymers whose dynamic properties are intimately coupled to nucleotide hydrolysis. In cells, the organization and dynamics of MTs are further tuned by post-translational modifications (PTMs), which control the ability of MT-associated proteins (MAPs) and molecular motors to engage MTs. Detyrosination is a PTM of α-tubulin, wherein its C-terminal tyrosine residue is enzymatically removed by either the vasohibin (VASH) or MT-associated tyrosine carboxypeptidase (MATCAP) peptidases. How these enzymes generate specific patterns of MT detyrosination in cells is not known. Here, we use a novel antibody-based probe to visualize the formation of detyrosinated MTs in real time and employ single-molecule imaging of VASH1 bound to its regulatory partner small-vasohibin binding protein (SVBP) to understand the process of MT detyrosination in vitro and in cells. We demonstrate that the activity, but not binding, of VASH1/SVBP is much greater on mimics of guanosine triphosphate (GTP)-MTs than on guanosine diphosphate (GDP)-MTs. Given emerging data showing that tubulin subunits in GTP-MTs are in expanded conformation relative to tubulin subunits in GDP-MTs, we reasoned that the lattice conformation of MTs is a key factor that gates the activity of VASH1/SVBP. We show that Taxol, a drug known to expand the MT lattice, promotes MT detyrosination and that CAMSAP2 and CAMSAP3 are two MAPs that spatially regulate detyrosination in cells. Collectively, our work shows that VASH1/SVBP detyrosination is regulated by the conformational state of tubulin in the MT lattice and that this is spatially determined in cells by the activity of MAPs.
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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.