ArticleLife science alliance2023
Preference of CAMSAP3 for expanded microtubule lattice contributes to stabilization of the minus end.
Article in Life science alliance, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Patronin promotes the formation of dynamic microtubule seeds in vivo.Journal of cell science · 2026Article
- MATCAP1 preferentially binds an expanded tubulin conformation to generate detyrosinated and ΔC2 α-tubulin.The EMBO journal · 2026Article
- The microtubule GTP-tubulin cap size is modulated during cell division.Molecular biology of the cell · 2026Article
- Article
- The microtubule GTP-tubulin cap size is modulated during cell division.bioRxiv : the preprint server for biology · 2026Article
- Accessibility of the unstructured α-tubulin C-terminal tail is controlled by microtubule lattice conformation.bioRxiv : the preprint server for biology · 2025Article
- Diverse microtubule-binding repeats regulate TPX2 activities at distinct locations within the spindle.The Journal of cell biology · 2025Article
- Article
- Phase separation of microtubule-binding proteins - implications for neuronal function and disease.Journal of cell science · 2024Review
- The GTP-tubulin cap is not the determinant of microtubule end stability in cells.Molecular biology of the cell · 2024Article
- CAMSAPs and nucleation-promoting factors control microtubule release from γ-TuRC.Nature cell biology · 2024Article
- Tau oligomerization on microtubules in health and disease.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Microtubule detyrosination by VASH1/SVBP is regulated by the conformational state of tubulin in the lattice.Current biology : CB · 2023Article
- Taxol acts differently on different tubulin isotypes.Communications biology · 2023Article
- A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle.The Journal of cell biology · 2023Article
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Authors and funding
2 authors.
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Abstract
CAMSAPs are proteins that show microtubule minus-end-specific localization, decoration, and stabilization. Although the mechanism for minus-end recognition via their C-terminal CKK domain has been well described in recent studies, it is unclear how CAMSAPs stabilize microtubules. Our several binding assays revealed that the D2 region of CAMSAP3 specifically binds to microtubules with the expanded lattice. To investigate the relationship between this preference and the stabilization effect of CAMSAP3, we precisely measured individual microtubule lengths and found that D2 binding expanded the microtubule lattice by ∼3%. Consistent with the notion that the expanded lattice is a common feature of stable microtubules, the presence of D2 slowed the microtubule depolymerization rate to ∼1/20, suggesting that the D2-triggered lattice expansion stabilizes microtubules. Combining these results, we propose that CAMSAP3 stabilizes microtubules by lattice expansion upon D2 binding, which further accelerates the recruitment of other CAMSAP3 molecules. Because only CAMSAP3 has D2 and the highest microtubule-stabilizing effect among mammalian CAMSAPs, our model also explains the molecular basis for the functional diversity of CAMSAP family members.
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