ArticleActa biochimica et biophysica Sinica2023
Cryo-EM of α-tubulin isotype-containing microtubules revealed a contracted structure of α4A/β2A microtubules.
Article in Acta biochimica et biophysica Sinica, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.Biophysical journal · 2026Article
- Screening the composition of tubulin isotypes reveals the most abundant TUBB4B for ciliary polarity in ependymal cells.Journal of molecular cell biology · 2026Article
- Investigating the Function of C‑Terminal Tails of Human Tubulin Isotypes in the Motility Regulation of Cytoplasmic Dynein.ACS omega · 2026Article
- TUBA8 promotes neuronal dendrite development through its 40th alanine.Journal of molecular cell biology · 2026Article
- Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays.Cytoskeleton (Hoboken, N.J.) · 2025Article
- A mutational hotspot inFrontiers in cellular neuroscience · 2025Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules are hollow α/β-tubulin heterodimeric polymers that play critical roles in cells. In vertebrates, both α- and β-tubulins have multiple isotypes encoded by different genes, which are intrinsic factors in regulating microtubule functions. However, the structures of microtubules composed of different tubulin isotypes, especially α-tubulin isotypes, remain largely unknown. Here, we purify recombinant tubulin heterodimers composed of different mouse α-tubulin isotypes, including α1A, α1C and α4A, with the β-tubulin isotype β2A. We further assemble and determine the cryo-electron microscopy (cryo-EM) structures of α1A/β2A, α1C/β2A, and α4A/β2A microtubules. Our structural analysis demonstrates that α4A/β2A microtubules exhibit longitudinal contraction between tubulin interdimers compared with α1A/β2A and α1C/β2A microtubules. Collectively, our findings reveal that α-tubulin isotype composition can tune microtubule structures, and also provide evidence for the "tubulin code" hypothesis.
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