ArticleThe Journal of biological chemistry1999
Lethal kinesin mutations reveal amino acids important for ATPase activation and structural coupling.
Article in The Journal of biological chemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 90 citations in OpenAlex.
- 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
- 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
- Microscopic interactions control a structural transition in active mixtures of microtubules and molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Dissipation and energy propagation across scales in an active cytoskeletal material.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- How neurons maintain their axons long-term: an integrated view of axon biology and pathology.Frontiers in neuroscience · 2023Review
- Kinesin-directed secretion of basement membrane proteins to a subdomain of the basolateral surface in Drosophila epithelial cells.Current biology : CB · 2022Article
- A stop or go switch: glycogen synthase kinase 3β phosphorylation of the kinesin 1 motor domain at Ser314 halts motility without detaching from microtubules.Development (Cambridge, England) · 2021Article
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- Optical flow analysis reveals that Kinesin-mediated advection impacts the orientation of microtubules in theMolecular biology of the cell · 2020Article
- TheThe Journal of cell biology · 2019Article
- Wolbachia and host germline components compete for kinesin-mediated transport to the posterior pole of the Drosophila oocyte.PLoS pathogens · 2018Article
- Autoinhibition of kinesin-1 is essential to the dendrite-specific localization of Golgi outposts.The Journal of cell biology · 2018Article
- Two kinesins drive anterograde neuropeptide transport.Molecular biology of the cell · 2017Article
- Active diffusion and advection in Drosophila oocytes result from the interplay of actin and microtubules.Nature communications · 2017Article
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- Emery-Dreifuss muscular dystrophy-linked genes and centronuclear myopathy-linked genes regulate myonuclear movement by distinct mechanisms.Molecular biology of the cell · 2017Article
- KIF1A mediates axonal transport of BACE1 and identification of independently moving cargoes in living SCG neurons.Traffic (Copenhagen, Denmark) · 2016Article
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- Role of kinesin-1-based microtubule sliding in Drosophila nervous system development.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
To study the relationship between conventional kinesin's structure and function, we identified 13 lethal mutations in the Drosophila kinesin heavy chain motor domain and tested a subset for effects on mechanochemistry. S246F is a moderate mutation that occurs in loop 11 between the ATP- and microtubule-binding sites. While ATP and microtubule binding appear normal, there is a 3-fold decrease in the rate of ATP turnover. This is consistent with the hypothesis that loop 11 provides a structural link that is important for the activation of ATP turnover by microtubule binding. T291M is a severe mutation that occurs in alpha-helix 5 near the center of the microtubule-binding surface. It impairs the microtubule-kinesin interaction and directly effects the ATP-binding pocket, allowing an increase in ATP turnover in the absence of microtubules. The T291M mutation may mimic the structure of a microtubule-bound, partially activated state. E164K is a moderate mutation that occurs at the beta-sheet 5a/loop 8b junction, remote from the ATP pocket. Surprisingly, it causes both tighter ATP-binding and a 2-fold decrease in ATP turnover. We propose that E164 forms an ionic bridge with alpha-helix 5 and speculate that it helps coordinate the alternating site catalysis of dimerized kinesin heavy chain motor domains.
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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.