Vasohibins encode tubulin detyrosinating activity
Open accessAbstract
Tubulin carboxypeptidase identity revealed: Enzymes of the α-tubulin detyrosination/tyrosination cycle create landmarks on microtubules that are essential for their multiple cellular functions and are altered in disease. Tubulin carboxypeptidases (TCPs) responsible for detyrosination have remained elusive for 40 years (see the Perspective by Akhmanova and Maiato). Aillaud et al. identified vasohibins as enzymes that perform the TCP function and found that their small interacting partner SBVP was essential for their activity. Vasohibin/SVBP complexes were involved in neuron polarization and brain cortex development. The authors also developed an inhibitor targeting this family of enzymes. Using a completely different strategy, Nieuwenhuis et al. also showed that vasohibins can remove the C-terminal tyrosine of α-tubulin. Science , this issue p. 1448 , p. 1453 ; see also p. 1381
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Induction of microtubule detyrosination by overexpressing VASH2-SVBP or MATCAP either did not impact the localization of GEF-H1 to microtubules or showed a slight increase in binding.
“Induction of microtubule detyrosination (removal of the C-terminal tyrosine of α-tubulin), another modification associated with microtubule stability 31 , by overexpressing the detyrosinating enzymes VASH2-SVBP or MATCAP 56-58 , either did not impact the localization of GEF-H1 to microtubules or showed a slight increase in binding (Extended Data Fig. 4b-e).”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [57]
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References 34 · Cited by 266
- Authors
- Nieuwenhuis, J., Adamopoulos, A., Bleijerveld, O. B., Mazouzi, A., Stickel, E., Celie, P., Altelaar, M., Knipscheer, P., Perrakis, A., Blomen, V. A., & Brummelkamp, T. R.
- Affiliations
- The Netherlands Cancer Institute (NL)
- Utrecht University (NL)
- University Medical Center Utrecht (NL)
- Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, Netherlands.
- Austrian Academy of Sciences (AT)
- Corresponding author
- Blomen, Vincent A.
- Brummelkamp, Thijn R.
- ORCID
- Venue
- Science
- Published
- 2017-12-15
- Volume
- 358
- Issue
- 6369
- Pages
- 1453-1456
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2770502839
- Cited by
- 266
- References
- 34
- Citations by year
- 2026: 20 · 2025: 28 · 2024: 41 · 2023: 32 · 2022: 41 · 2021: 29 · 2020: 33 · 2019: 25 · 2018: 14 · 2017: 3
- FWCI
- 11.23
- Type
- journal article
- Language
- en
- Open access
- green
- dspace.library.uu.nl
- Licence
- other-oa
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- KNAW research portal (Royal Academy of Art and Sciences (KNAW)) (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- KNAW Research Portal (The Royal Netherlands Academy of Arts and Sciences) (submittedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Physical Sciences › Chemistry › Organic Chemistry › Synthesis and biological activity
- Keywords
- vasohibin, vasohibin-1, vasohibin-2, tubulin detyrosination, alpha-tubulin, post-translational modification, angiogenesis regulators, cell type-dependent regulation
- MeSH terms
- Carboxypeptidases, Carrier Proteins, Haploidy, Humans, Tubulin, Tyrosine, Cell Cycle Proteins, Neovascularization, Physiologic, Angiogenic Proteins, Biocatalysis
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