ArticleProceedings of the National Academy of Sciences of the United States of America2022
Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 6 citations in OpenAlex.
- Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends.The Journal of cell biology · 2025Article
- HURP binding to the vinca domain of β-tubulin accounts for cancer drug resistance.Nature communications · 2024Article
- Examining Heterodimerization by Aryl C-N Coupling in Dynemicin Biosynthesis.ACS chemical biology · 2023Article
- Computational Approaches to the Rational Design of Tubulin-Targeting Agents.Biomolecules · 2023Review
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9 authors at 2 institutions in 1 country.
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Abstract
Microtubule dynamics is regulated by various cellular proteins and perturbed by small-molecule compounds. To what extent the mechanism of the former resembles that of the latter is an open question. We report here structures of tubulin bound to the PN2-3 domain of CPAP, a protein controlling the length of the centrioles. We show that an α-helix of the PN2-3 N-terminal region binds and caps the longitudinal surface of the tubulin β subunit. Moreover, a PN2-3 N-terminal stretch lies in a β-tubulin site also targeted by fungal and bacterial peptide-like inhibitors of the vinca domain, sharing a very similar binding mode with these compounds. Therefore, our results identify several characteristic features of cellular partners that bind to this site and highlight a structural convergence of CPAP with small-molecule inhibitors of microtubule assembly.
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