Tubulin Posttranslational Modifications and Emerging Links to Human Disease
Open accessAbstract
Tubulin posttranslational modifications are currently emerging as important regulators of the microtubule cytoskeleton and thus have a strong potential to be implicated in a number of disorders. Here, we review the latest advances in understanding the physiological roles of tubulin modifications and their links to a variety of pathologies.
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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 [31]
The indexed passage on detyrosination (section labeled Abstract; page unavailable) says that vasohibins catalyze tubulin detyrosination and cites work identifying vasohibins/SVBP as tubulin carboxypeptidases. It does not report VASH2-SVBP or MATCAP overexpression experiments, or whether detyrosination changes GEF-H1 localization or binding to microtubules; those results are attributed to the citing paper’s Extended Data Fig. 4b–e. (LLM, conf=0.82)
Experimental — accuracy not yet measuredMicrotubule stabilization can potentially affect microtubule-associated components of signalling cascades by altering their turnover and tubulin post-translational modifications.
“However, microtubule stabilization can potentially affect microtubule-associated components of signalling cascades by altering their turnover and tubulin post-translational modifications 31 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [31]
The passage beginning “In living cells” (indexed as Abstract; no page supplied) says tubulin post-translational modifications can affect microtubule stability and interactions with microtubule-associated proteins. It does not say that stabilizing microtubules alters their turnover or modifications, or that this affects components of signalling cascades. (LLM, conf=0.78)
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- Authors
- Magiera, M. M., Singh, P., Gadadhar, S., & Janke, C.
- Affiliations
- Université Paris-Sud (FR)
- Corresponding author
- Magiera, Maria M.
- Janke, Carsten
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2018-05
- Volume
- 173
- Issue
- 6
- Pages
- 1323-1327
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2807269502
- Cited by
- 169
- References
- 51
- Citations by year
- 2026: 11 · 2025: 14 · 2024: 17 · 2023: 21 · 2022: 18 · 2021: 17 · 2020: 36 · 2019: 28 · 2018: 7
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- the French National Research Agency
- ANR (ANR-10-LBX-0038, ANR-10-IDEX-0001-02 PSL, ANR-12-BSV2-0007)
- Institut National du Cancer
- INCA (2013-1-PL BIO-02-ICR-1, 2014-PL BIO-11-ICR-1)
- EMBO (ASTF 148-2015)
- Fondation Vaincre Alzheimer (FR-16055p.)
- Ligue contre le Cancer
- 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
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tubulin post-translational modifications, microtubule cytoskeleton, tubulin acetylation, microtubule dynamics, human disease, neurodegenerative diseases, cancer
- MeSH terms
- Animals, Blood Platelets, Cilia, Cytoskeleton, Flagella, Heart Diseases, Humans, Microtubules, Mutation, Phenotype, Protein Processing, Post-Translational, Risk Factors, Tubulin, Neurodegenerative Diseases, Mice
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