ArticleMolecular biology of the cell2002
Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Tubulin isotype regulation maintains asymmetric requirement for α-tubulin over β-tubulin.The Journal of cell biology · 2023Article
- Quantifying the Monomer-Dimer Equilibrium of Tubulin with Mass Photometry.Journal of molecular biology · 2020Article
- Effect of Cyclic Stretch on Neuron Reorientation and Axon Outgrowth.Frontiers in bioengineering and biotechnology · 2020Article
- All tubulins are not alike: Heterodimer dissociation differs among different biological sources.The Journal of biological chemistry · 2019Article
- Resistance to anti-tubulin agents: From vinca alkaloids to epothilones.Cancer drug resistance (Alhambra, Calif.) · 2019Review
- Weak protein-protein interactions in live cells are quantified by cell-volume modulation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Revisiting the tubulin cofactors and Arl2 in the regulation of soluble αβ-tubulin pools and their effect on microtubule dynamics.Molecular biology of the cell · 2017Article
- Tubulin Dimer Reversible Dissociation: AFFINITY, KINETICS, AND DEMONSTRATION OF A STABLE MONOMER.The Journal of biological chemistry · 2016Article
- Article
- Challenges and dreams: physics of weak interactions essential to life.Molecular biology of the cell · 2014Article
- Article
- Tubulin-specific chaperones: components of a molecular machine that assembles the α/β heterodimer.Methods in cell biology · 2013Article
- Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers.Biochemistry · 2011Article
- Bacterial tubulin distinct loop sequences and primitive assembly properties support its origin from a eukaryotic tubulin ancestor.The Journal of biological chemistry · 2011Article
- Dimeric states of neural- and epithelial-cadherins are distinguished by the rate of disassembly.Biochemistry · 2011Article
- Emerging roles for tubulin folding cofactors at the centrosome.Communicative & integrative biology · 2010Article
- Article
- Structural mass spectrometry of the alpha beta-tubulin dimer supports a revised model of microtubule assembly.Biochemistry · 2009Article
- Tubulin heterodimers remain functional for one cell cycle after the inactivation of tubulin-folding cofactor D in fission yeast cells.Yeast (Chichester, England) · 2009Article
- Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch.Journal of molecular biology · 2008Article
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2 authors.
Funding
Abstract
The finding that exchange of tubulin subunits between tubulin dimers (alpha-beta + alpha'beta' <--> alpha'beta + alphabeta') does not occur in the absence of protein cofactors and GTP hydrolysis conflicts with the assumption that pure tubulin dimer and monomer are in rapid equilibrium. This assumption underlies the many physical chemical measurements of the K(d) for dimer dissociation. To resolve this discrepancy we used surface plasmon resonance to determine the rate constant for dimer dissociation. The half-time for dissociation was approximately 9.6 h with tubulin-GTP, 2.4 h with tubulin-GDP, and 1.3 h in the absence of nucleotide. A Kd equal to 10(-11) M was calculated from the measured rate for dissociation and an estimated rate for association. Dimer dissociation was found to be reversible, and dimer formation does not require GTP hydrolysis or folding information from protein cofactors, because 0.2 microM tubulin-GDP incubated for 20 h was eluted as dimer when analyzed by size exclusion chromatography. Because 20 h corresponds to eight half-times for dissociation, only monomer would be present if dissociation were an irreversible reaction and if dimer formation required GTP or protein cofactors. Additional evidence for a 10(-11) M K(d) was obtained from gel exclusion chromatography studies of 0.02-2 nM tubulin-GDP. The slow dissociation of the tubulin dimer suggests that protein tubulin cofactors function to catalyze dimer dissociation, rather than dimer assembly. Assuming N-site-GTP dissociation is from monomer, our results agree with the 16-h half-time for N-site GTP in vitro and 33 h half-life for tubulin N-site-GTP in CHO cells.
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