ArticlebioRxiv : the preprint server for biology2026
Role of α-tubulin helix 11' in heterodimer conformation and microtubule dynamics.
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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3 authors.
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Abstract
Tubulin heterodimers transition from a curved conformation in solution to straight conformation when assembled into the microtubule lattice. Many proteins and small molecules alter microtubule dynamics by binding and stabilizing the curved or straight conformations; however, we have a poor understanding of the regions of the tubulin heterodimer that contribute to this transition and whether these conformations represent sources of phenotypic variation in human disease and across species. We previously identified a role for α-tubulin helix 11' (H11') in the curved-to-straight transition. Using computational simulations and tubulin mutants in budding yeast, we show that H11' variants associated with human disease destabilize the curved conformation of the heterodimer and disrupt α-tubulin function in cells. Comparing α-tubulin sequences across eukaryotes demonstrates strong conservation of H11' with the exception of several α-tubulin isotypes expressed during mitosis in the amoebae
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