ArticleThe Journal of biological chemistry2016
Tubulin Dimer Reversible Dissociation: AFFINITY, KINETICS, AND DEMONSTRATION OF A STABLE MONOMER.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Tubulin isotype regulation maintains asymmetric requirement for α-tubulin over β-tubulin.The Journal of cell biology · 2023Article
- Protein complexes and neighborhoods driving autophagy.Autophagy · 2021Review
- Molecular mechanisms underlying microtubule growth dynamics.Current biology : CB · 2021Review
- Quantifying the Monomer-Dimer Equilibrium of Tubulin with Mass Photometry.Journal of molecular biology · 2020Article
- Structural basis of the strong cell-cell junction formed by cadherin-23.The FEBS journal · 2019Article
- All tubulins are not alike: Heterodimer dissociation differs among different biological sources.The Journal of biological chemistry · 2019Article
- Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.Nature protocols · 2017Article
- A Trimer Consisting of the Tubulin-specific Chaperone D (TBCD), Regulatory GTPase ARL2, and β-Tubulin Is Required for Maintaining the Microtubule Network.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Tubulins are evolutionarily conserved proteins that reversibly polymerize and direct intracellular traffic. Of the tubulin family only αβ-tubulin forms stable dimers. We investigated the monomer-dimer equilibrium of rat brain αβ-tubulin using analytical ultracentrifugation and fluorescence anisotropy, observing tubulin in virtually fully monomeric and dimeric states. Monomeric tubulin was stable for a few hours and exchanged into preformed dimers, demonstrating reversibility of dimer dissociation. Global analysis combining sedimentation velocity and fluorescence anisotropy yielded Kd = 84 (54-123) nm Dimer dissociation kinetics were measured by analyzing the shape of the sedimentation boundary and by the relaxation of fluorescence anisotropy following rapid dilution of labeled tubulin, yielding koff in the range 10(-3)-10(-2) s(-1) Thus, tubulin dimers reversibly dissociate with moderately fast kinetics. Monomer-monomer association is much less sensitive than dimer-dimer association to solution changes (GTP/GDP, urea, and trimethylamine oxide).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.