ArticlePLoS computational biology2019
Mechanical properties of tubulin intra- and inter-dimer interfaces and their implications for microtubule dynamic instability.
Article in PLoS computational biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Integrative AI-assisted modeling suggests CPPF binding at a composite α/β-tubulin interface pocket dominated by β-tubulin contacts.PLoS computational biology · 2026Article
- Single-molecule microtubule dynamics measurements reveal an intermediate state and clarify the role of nucleotide.Nature communications · 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
- Structures of Native Doublet Microtubules from Trichomonas vaginalis Reveal Parasite-Specific Proteins.Nature communications · 2025Article
- Exploring tubulin-paclitaxel binding modes through extensive molecular dynamics simulations.Scientific reports · 2025Article
- Structures of Native Doublet Microtubules fromResearch square · 2024Article
- Structural insights into the mechanism of GTP initiation of microtubule assembly.Nature communications · 2023Article
- In silico analysis of TUBA4A mutations in Amyotrophic Lateral Sclerosis to define mechanisms of microtubule disintegration.Scientific reports · 2023Article
- Review
- CLASP2 recognizes tubulins exposed at the microtubule plus-end in a nucleotide state-sensitive manner.Science advances · 2023Article
- The tubulin database: Linking mutations, modifications, ligands and local interactions.PloS one · 2023Article
- Beyond the GTP-cap: Elucidating the molecular mechanisms of microtubule catastrophe.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- High-pressure crystallography shows noble gas intervention into protein-lipid interaction and suggests a model for anaesthetic action.Communications biology · 2022Article
- A Review of the Recent Developments of Molecular Hybrids Targeting Tubulin Polymerization.International journal of molecular sciences · 2022Review
- Bending-torsional elasticity and energetics of the plus-end microtubule tip.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- H-ABC- and dystonia-causingScience advances · 2022Article
- Role of microtubule dynamics in Wallerian degeneration and nerve regeneration after peripheral nerve injury.Neural regeneration research · 2022Article
- Long Noncoding RNA and mRNA m6A Modification Analyses of Periodontal Ligament Stem Cells from the Periodontitis Microenvironment Exposed to Static Mechanical Strain.Stem cells international · 2022Article
- Regulation of microtubule dynamics, mechanics and function through the growing tip.Nature reviews. Molecular cell biology · 2021Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thirteen tubulin protofilaments, made of αβ-tubulin heterodimers, interact laterally to produce cytoskeletal microtubules. Microtubules exhibit the striking property of dynamic instability, manifested in their intermittent growth and shrinkage at both ends. This behavior is key to many cellular processes, such as cell division, migration, maintenance of cell shape, etc. Although assembly and disassembly of microtubules is known to be linked to hydrolysis of a guanosine triphosphate molecule in the pocket of β-tubulin, detailed mechanistic understanding of corresponding conformational changes is still lacking. Here we take advantage of the recent generation of in-microtubule structures of tubulin to examine the properties of protofilaments, which serve as important microtubule assembly and disassembly intermediates. We find that initially straight tubulin protofilaments, relax to similar non-radially curved and slightly twisted conformations. Our analysis further suggests that guanosine triphosphate hydrolysis primarily affects the flexibility and conformation of the inter-dimer interface, without a strong impact on the shape or flexibility of αβ-heterodimer. Inter-dimer interfaces are significantly more flexible compared to intra-dimer interfaces. We argue that such a difference in flexibility could be key for distinct stability of the plus and minus microtubule ends. The higher flexibility of the inter-dimer interface may have implications for development of pulling force by curving tubulin protofilaments during microtubule disassembly, a process of major importance for chromosome motions in mitosis.
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