ArticleThe Journal of biological chemistry2006
Dimeric Eg5 maintains processivity through alternating-site catalysis with rate-limiting ATP hydrolysis.
Article in The Journal of biological chemistry, 2006. 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.
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Measurement of Nucleotide Hydrolysis Using Fluorescent Biosensors for Phosphate.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Small molecule allosteric uncoupling of microtubule depolymerase activity from motility in human Kinesin-5 during mitotic spindle assembly.Scientific reports · 2019Article
- Altered chemomechanical coupling causes impaired motility of the kinesin-4 motors KIF27 and KIF7.The Journal of cell biology · 2018Article
- Collective Force Regulation in Anti-parallel Microtubule Gliding by Dimeric Kif15 Kinesin Motors.Current biology : CB · 2017Article
- Src family kinase phosphorylation of the motor domain of the human kinesin-5, Eg5.Cytoskeleton (Hoboken, N.J.) · 2017Article
- The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.The Journal of biological chemistry · 2017Article
- The Kinesin-5 Chemomechanical Cycle Is Dominated by a Two-heads-bound State.The Journal of biological chemistry · 2016Article
- Motile properties of the bi-directional kinesin-5 Cin8 are affected by phosphorylation in its motor domain.Scientific reports · 2016Article
- Kinesin-5 inhibitor resistance is driven by kinesin-12.The Journal of cell biology · 2016Article
- The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Kinesin-5 is a microtubule polymerase.Nature communications · 2015Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Kinesin-2 KIF3AB exhibits novel ATPase characteristics.The Journal of biological chemistry · 2014Article
- Mechanism and regulation of kinesin-5, an essential motor for the mitotic spindle.Biology of the cell · 2014Review
- Review
- The ATPase pathway that drives the kinesin-14 Kar3Vik1 powerstroke.The Journal of biological chemistry · 2012Article
- Microtubule capture by mitotic kinesin centromere protein E (CENP-E).The Journal of biological chemistry · 2012Article
- The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.Biophysical journal · 2011Article
- Kinesin Kar3Cik1 ATPase pathway for microtubule cross-linking.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Eg5/KSP is a homotetrameric, Kinesin-5 family member whose ability to cross-link microtubules has associated it with mitotic spindle assembly and dynamics for chromosome segregation. Transient-state kinetic methodologies have been used to dissect the mechanochemical cycle of a dimeric motor, Eg5-513, to better understand the cooperative interactions that modulate processive stepping. Microtubule association, ADP release, and ATP binding are all fast steps in the pathway. However, the acid-quench analysis of the kinetics of ATP hydrolysis with substrate in excess of motor was unable to resolve a burst of product formation during the first turnover event. In addition, the kinetics of P(i) release and ATP-promoted microtubule-Eg5 dissociation were observed to be no faster than the rate of ATP hydrolysis. In combination the data suggest that dimeric Eg5 is the first kinesin motor identified to have a rate-limiting ATP hydrolysis step. Furthermore, several lines of evidence implicate alternating-site catalysis as the molecular mechanism underlying dimeric Eg5 processivity. Both mantATP binding and mantADP release transients are biphasic. Analysis of ATP hydrolysis through single turnover assays indicates a surprising substrate concentration dependence, where the observed rate is reduced by half when substrate concentration is sufficiently high to require both motor domains of the dimer to participate in the reaction.
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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 OpenQuestion graph.