Posttranslational modification of microtubules by the MATCAP detyrosinase
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The detyrosination-tyrosination cycle involves the removal and religation of the C-terminal tyrosine of α-tubulin and is implicated in cognitive, cardiac, and mitotic defects. The vasohibin–small vasohibin-binding protein (SVBP) complex underlies much, but not all, detyrosination. We used haploid genetic screens to identify an unannotated protein, microtubule associated tyrosine carboxypeptidase (MATCAP), as a remaining detyrosinating enzyme. X-ray crystallography and cryo–electron microscopy structures established MATCAP’s cleaving mechanism, substrate specificity, and microtubule recognition. Paradoxically, whereas abrogation of tyrosine religation is lethal in mice, codeletion of MATCAP and SVBP is not. Although viable, defective detyrosination caused microcephaly, associated with proliferative defects during neurogenesis, and abnormal behavior. Thus, MATCAP is a missing component of the detyrosination-tyrosination cycle, revealing the importance of this modification in brain formation.
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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 [58]
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Anti-Breast Cancer Properties and In Vivo Safety Profile of a Bis-Carbazole Derivative
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Spotted around the web: Sex differences in microglia, Google searches, Kavli Prize
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- Authors
- Landskron, L., Bak, J., Adamopoulos, A., Kaplani, K., Moraiti, M., van den Hengel, L. G., Song, J.-Y., Bleijerveld, O. B., Nieuwenhuis, J., Heidebrecht, T., Henneman, L., Moutin, M.-J., Barisic, M., Taraviras, S., Perrakis, A., & Brummelkamp, T. R.
- Affiliations
- The Netherlands Cancer Institute (NL)
- University of Patras (GR)
- Oncode Institute, Division of Biochemistry, Netherlands Cancer Institute, 1066CX Amsterdam, Netherlands.
- Centre National de la Recherche Scientifique (FR)
- Cell Division and Cytoskeleton, Danish Cancer Society Research Center (DCRC), 2100 Copenhagen, Denmark.
- Corresponding author
- Brummelkamp, Thijn R.
- ORCID
- Venue
- Science
- Published
- 2022-05-20
- Volume
- 376
- Issue
- 6595
- Pages
- eabn6020-eabn6020
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W4225121910
- Cited by
- 78
- References
- 66
- Citations by year
- 2026: 13 · 2025: 23 · 2024: 15 · 2023: 16 · 2022: 11
- FWCI
- 8.83
- Type
- journal article
- Language
- en
- Open access
- Licence
- other-oa
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, other-oa)
- HAL (submittedVersion, other-oa)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, other-oa)
- Funders
- Agence Nationale de la Recherche (ANR-20-CE16-0021)
- Lundbeckfonden (R215‐2015-4081)
- Novo Nordisk Fonden (NNF19OC0058504)
- 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
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- microtubule detyrosination, microcephaly, neurogenesis, brain development
- MeSH terms
- Animals, Carboxypeptidases, Humans, Microtubule-Associated Proteins, Microtubules, Protein Processing, Post-Translational, Tubulin, Tyrosine, Crystallography, X-Ray, Cryoelectron Microscopy, Mice
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