ArticleThe Journal of biological chemistry2003
A kinesin switch I arginine to lysine mutation rescues microtubule function.
Article in The Journal of biological chemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
- The kinesin-4 protein KIF27 forms a cytoskeletal scaffold at the transition zone to promote motile cilia structural integrity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Interior modification of Macrobrachium rosenbergii nodavirus-like particle enhances encapsulation of VP37-dsRNA against shrimp white spot syndrome infection.BMC veterinary research · 2024Article
- Plus and minus ends of microtubules respond asymmetrically to kinesin binding by a long-range directionally driven allosteric mechanism.Science advances · 2022Article
- Selective Recognition of Amino Acids and Peptides by Small Supramolecular Receptors.Molecules (Basel, Switzerland) · 2020Review
- Fast-forward genetics by radiation hybrids to saturate the locus regulating nuclear-cytoplasmic compatibility in Triticum.Plant biotechnology journal · 2016Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Kinesin processivity is gated by phosphate release.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Microtubule-sliding activity of a kinesin-8 promotes spindle assembly and spindle-length control.Nature cell biology · 2013Article
- Mitotic spindle assembly around RCC1-coated beads in Xenopus egg extracts.PLoS biology · 2011Article
- Kinesin Kar3Cik1 ATPase pathway for microtubule cross-linking.The Journal of biological chemistry · 2011Article
- Loop L5 acts as a conformational latch in the mitotic kinesin Eg5.The Journal of biological chemistry · 2011Article
- Processive movement by a kinesin heterodimer with an inactivating mutation in one head.Biochemistry · 2008Article
- To step or not to step? How biochemistry and mechanics influence processivity in Kinesin and Eg5.Current opinion in cell biology · 2007Review
- Article
- Kinesin's second step.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Switch I and II are key active site structural elements of kinesins, myosins, and G-proteins. Our analysis of a switch I mutant (R210A) in Drosophila melanogaster kinesin showed a reduction in microtubule affinity, a loss in cooperativity between the motor domains, and an ATP hydrolysis defect leading to aberrant detachment from the microtubule. To investigate the conserved arginine in switch I further, a lysine substitution mutant was generated. The R210K dimeric motor has lost the ability to hydrolyze ATP; however, it has rescued microtubule function. Our results show that R210K has restored microtubule association kinetics, microtubule affinity, ADP release kinetics, and motor domain cooperativity. Moreover, the active site at head 1 is able to distinguish ATP, ADP, and AMP-PNP to signal head 2 to bind the microtubule and release mantADP with kinetics comparable with wild-type. Therefore, the structural pathway of communication from head 1 to head 2 is restored, and head 2 can respond to this signal by binding the microtubule and releasing mantADP. Structural modeling revealed that lysine could retain some of the hydrogen bonds made by arginine but not all, suggesting a structural hypothesis for the ability of lysine to rescue microtubule function in the Arg210 mutant.
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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.