ArticleBiophysical journal2011
The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5.Journal of chemical information and modeling · 2026Article
- Mitotic Functions and Characters of KIF11 in Cancers.Biomolecules · 2024Review
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- MD simulation-based screening approach identified tolvaptan as a potential inhibitor of Eg5.Molecular diversity · 2023Article
- Using a comprehensive approach to investigate the interaction between Kinesin-5/Eg5 and the microtubule.Computational and structural biotechnology journal · 2022Article
- Cryo-EM structure of a microtubule-bound parasite kinesin motor and implications for its mechanism and inhibition.The Journal of biological chemistry · 2021Article
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Vanadocene dichloride induces apoptosis in HeLa cells through depolymerization of microtubules and inhibition of Eg5.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Small molecule allosteric uncoupling of microtubule depolymerase activity from motility in human Kinesin-5 during mitotic spindle assembly.Scientific reports · 2019Article
- Dual inhibition of Kif15 by oxindole and quinazolinedione chemical probes.Bioorganic & medicinal chemistry letters · 2019Article
- Synthetic-Evolution Reveals Narrow Paths to Regulation of theInternational journal of biological sciences · 2019Article
- The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.The Journal of biological chemistry · 2017Article
- Src family kinase phosphorylation of the motor domain of the human kinesin-5, Eg5.Cytoskeleton (Hoboken, N.J.) · 2017Article
- Recent findings and future directions for interpolar mitotic kinesin inhibitors in cancer therapy.Future medicinal chemistry · 2016Review
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Comprehensive structural model of the mechanochemical cycle of a mitotic motor highlights molecular adaptations in the kinesin family.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mechanism and regulation of kinesin-5, an essential motor for the mitotic spindle.Biology of the cell · 2014Review
- Review
- Loop L5 assumes three distinct orientations during the ATPase cycle of the mitotic kinesin Eg5: a transient and time-resolved fluorescence study.The Journal of biological chemistry · 2013Article
- Intrinsic Disorder in the Kinesin Superfamily.Biophysical reviews · 2013Article
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Authors and funding
8 authors.
Funding
Abstract
Eg5 is a homotetrameric kinesin-5 motor protein that generates outward force on the overlapping, antiparallel microtubules (MTs) of the mitotic spindle. Upon binding an MT, an Eg5 dimer releases one ADP molecule, undergoes a slow (∼0.5 s(-1)) isomerization, and finally releases a second ADP, adopting a tightly MT-bound, nucleotide-free (APO) conformation. This conformation precedes ATP binding and stepping. Here, we use mutagenesis, steady-state and pre-steady-state kinetics, motility assays, and electron paramagnetic resonance spectroscopy to examine Eg5 monomers and dimers as they bind MTs and initiate stepping. We demonstrate that a critical element of Eg5, loop 5 (L5), accelerates ADP release during the initial MT-binding event. Furthermore, our electron paramagnetic resonance data show that L5 mediates the slow isomerization by preventing Eg5 dimer heads from binding the MT until they release ADP. Finally, we find that Eg5 having a seven-residue deletion within L5 can still hydrolyze ATP and move along MTs, suggesting that L5 is not required to accelerate subsequent steps of the motor along the MT. Taken together, these properties of L5 explain the kinetic effects of L5-directed inhibition on Eg5 activity and may direct further interventions targeting Eg5 activity.
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