ArticleProtein science : a publication of the Protein Society2020
Insights into allosteric control of microtubule dynamics from a buried β-tubulin mutation that causes faster growth and slower shrinkage.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 13 citations in OpenAlex.
- Single-molecule microtubule dynamics measurements reveal an intermediate state and clarify the role of nucleotide.Nature communications · 2025Article
- Purification, Fluorescent Labeling, and Detyrosination of Mammalian Cell Tubulin for Biochemical Assays.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Mechanisms of microtubule dynamics from single-molecule measurements.bioRxiv : the preprint server for biology · 2025Article
- Microtubule dynamics are defined by conformations and stability of clustered protofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025Review
- Poxvirus A51R proteins regulate microtubule stability and antagonize a cell-intrinsic antiviral response.Cell reports · 2024Article
- CLASPs stabilize the pre-catastrophe intermediate state between microtubule growth and shrinkage.The Journal of cell biology · 2023Article
- The tubulin database: Linking mutations, modifications, ligands and local interactions.PloS one · 2023Article
- Reconstituting Microtubules: A Decades-Long Effort From Building Block Identification to the Generation of Recombinant α/β-Tubulin.Frontiers in cell and developmental biology · 2022Review
- A Multipronged Approach Establishes Covalent Modification of β-Tubulin as the Mode of Action of Benzamide Anti-cancer Toxins.Journal of medicinal chemistry · 2020Article
- Article
- Insights into allosteric control of microtubule dynamics from a buried β-tubulin mutation that causes faster growth and slower shrinkage.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
αβ-tubulin subunits cycle through a series of different conformations in the polymer lattice during microtubule growing and shrinking. How these allosteric responses to different tubulin:tubulin contacts contribute to microtubule dynamics, and whether the contributions are evolutionarily conserved, remains poorly understood. Here, we sought to determine whether the microtubule-stabilizing effects (slower shrinking) of the β:T238A mutation we previously observed using yeast αβ-tubulin would generalize to mammalian microtubules. Using recombinant human microtubules as a model, we found that the mutation caused slow microtubule shrinking, indicating that this effect of the mutation is indeed conserved. However, unlike in yeast, β:T238A human microtubules grew faster than wild-type and the mutation did not appear to attenuate the conformational change associated with guanosine 5'-triphosphate (GTP) hydrolysis in the lattice. We conclude that the assembly-dependent conformational change in αβ-tubulin can contribute to determine the rates of microtubule growing as well as shrinking. Our results also suggest that an allosteric perturbation like the β:T238A mutation can alter the behavior of terminal subunits without accompanying changes in the conformation of fully surrounded subunits in the body of the microtubule.
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