ArticleBiochemistry2004
Microtubule-kinesin interface mutants reveal a site critical for communication.
Article in Biochemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- 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
- A synthetic ancestral kinesin-13 depolymerizes microtubules faster than any natural depolymerizing kinesin.Open biology · 2022Article
- The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.The Journal of biological chemistry · 2017Article
- Common general anesthetic propofol impairs kinesin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- 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
- The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.Biophysical journal · 2011Article
- Article
- Interaction of kinesin motors, microtubules, and MAPs.Journal of muscle research and cell motility · 2006Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Strict coordination of the two motor domains of kinesin is required for driving the processive movement of organelles along microtubules. Glutamate 164 of the kinesin heavy chain was shown to be critical for kinesin function through in vivo genetics in Drosophila melanogaster. The mutant motor E164K exhibited reduced steady-state ATPase activity and higher affinity for both ATP and microtubules. Moreover, an alanine substitution at this position (E164A) caused similar defects. It became stalled on the microtubule and was unable to bind and hydrolyze ATP at the second motor domain. Glu(164), which has been conserved through evolution, is located at the motor-microtubule interface close to key residues on helix alpha12 of beta-tubulin. We explored further the contributions of Glu(164) to motor function using several site-directed mutant proteins: E164K, E164N, E164D, E164Q, and D165A. The results indicate that the microtubule-E164K complex can only bind and hydrolyze one ATP. ATP with increased salt was able to dissociate a population of E164K motors from the microtubule but could not dissociate E164A. We tested the basis of the stabilized microtubule interaction with E164K, E164N, and E164A. The results provide new insights about the motor-microtubule interface and the pathway of communication for processive motility.
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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.