ArticleScience advances2023
A family of carboxypeptidases catalyzing α- and β-tubulin tail processing and deglutamylation.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- C-Terminal Tail Elongation Adds a New Dimension to the Tubulin Code.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Condensation of MATCAP promotes CENP-E-dependent chromosome congression in mitosis.Nature communications · 2026Article
- Prognostic, diagnostic and therapeutic value of the cancer tubulin code.Cancer metastasis reviews · 2026Review
- MATCAP1 preferentially binds an expanded tubulin conformation to generate detyrosinated and ΔC2 α-tubulin.The EMBO journal · 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
- Suppressing microtubule detyrosination augments adeno-associated virus 2 endosomal escape and gene delivery.Journal of cell science · 2025Article
- Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation.bioRxiv : the preprint server for biology · 2025Article
- Mechanistic insights into TTLL11 polyglutamylase-mediated primary tubulin chain elongation.Science advances · 2025Article
- Non-canonical CDK6 activity promotes cilia disassembly by suppressing axoneme polyglutamylation.The Journal of cell biology · 2025Article
- Emerging roles for tubulin PTMs in neuronal function and neurodegenerative disease.Current opinion in neurobiology · 2025Review
- Tubulin detyrosination shapesProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Systematic Identification of Microtubule Posttranslational Modification "Readers" by Quantitative Proteomics.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Consciousness and the Axon Initial Segment.Integrative psychological & behavioral science · 2024Article
- Spatial arrangement, polarity, and posttranslational modifications of the microtubule system in the Drosophila eye.Cell and tissue research · 2024Article
- Tubulin glycylation controls ciliary motility through modulation of outer-arm dyneins.Molecular biology of the cell · 2024Article
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9 authors.
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Abstract
Tubulin posttranslational modifications represent an important mechanism involved in the regulation of microtubule functions. The most widespread among them are detyrosination, α∆2-tubulin, and polyglutamylation. Here, we describe a family of tubulin-modifying enzymes composed of two closely related proteins, KIAA0895L and KIAA0895, which have tubulin metallocarboxypeptidase activity and thus were termed TMCP1 and TMCP2, respectively. We show that TMCP1 (also known as MATCAP) acts as α-tubulin detyrosinase that also catalyzes α∆2-tubulin. In contrast, TMCP2 preferentially modifies βI-tubulin by removing three amino acids from its C terminus, generating previously unknown βI∆3 modification. We show that βI∆3-tubulin is mostly found on centrioles and mitotic spindles and in cilia. Moreover, we demonstrate that TMCPs also remove posttranslational polyglutamylation and thus act as tubulin deglutamylases. Together, our study describes the identification and comprehensive biochemical analysis of a previously unknown type of tubulin-modifying enzymes involved in the processing of α- and β-tubulin C-terminal tails and deglutamylation.
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