ArticleThe Journal of cell biology1996
Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 100 citations in OpenAlex.
- The unconventional regulation of non-muscle myosins.Biophysical reviews · 2026Article
- A FRET assay to monitor different structural states of human β-cardiac myosin including the interacting-heads motif.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Force-insensitive myosin-I enhances endocytosis robustness through actin network-scale collective ratcheting.Molecular biology of the cell · 2025Article
- Pathophysiology of human hearing loss associated with variants in myosins.Frontiers in physiology · 2024Review
- Class I Myosins, molecular motors involved in cell migration and cancer.Cell adhesion & migration · 2022Article
- Emergent spatiotemporal dynamics of the actomyosin network in the presence of chemical gradients.Integrative biology : quantitative biosciences from nano to macro · 2019Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- Use of stopped-flow fluorescence and labeled nucleotides to analyze the ATP turnover cycle of kinesins.Journal of visualized experiments : JoVE · 2014Article
- Nuclear myosin 1c facilitates the chromatin modifications required to activate rRNA gene transcription and cell cycle progression.PLoS genetics · 2013Article
- Regulation and control of myosin-I by the motor and light chain-binding domains.Trends in cell biology · 2013Review
- Shaking the myosin family tree: biochemical kinetics defines four types of myosin motor.Seminars in cell & developmental biology · 2011Review
- A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity.Biochemistry · 2011Article
- Impact of actin glutathionylation on the actomyosin-S1 ATPase.Biochemistry · 2009Article
- The three-dimensional dynamics of actin waves, a model of cytoskeletal self-organization.Biophysical journal · 2009Article
- Kinetic and equilibrium analysis of the myosin ATPase.Methods in enzymology · 2009Article
- Temperature dependence of nucleotide association and kinetic characterization of myo1b.Biochemistry · 2006Article
- The yeast actin cytoskeleton: from cellular function to biochemical mechanism.Microbiology and molecular biology reviews : MMBR · 2006Review
- Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains.The Journal of cell biology · 2001Article
- The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-based motors.The Journal of cell biology · 2001Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Acanthamoeba myosin-IA and myosin-IB are single-headed molecular motors that may play an important role in membrane-based motility. To better define the types of motility that myosin-IA and myosin IB can support, we determined the rate constants for key steps on the myosin-I ATPase pathway using fluorescence stopped-flow, cold-chase, and rapid-quench techniques. We determined the rate constants for ATP binding, ATP hydrolysis, actomyosin-I dissociation, phosphate release, and ADP release. We also determined equilibrium constants for myosin-I binding to actin filaments, ADP binding to actomyosin-I, and ATP hydrolysis. These rate constants define an ATPase mechanism in which (a) ATP rapidly dissociates actomyosin-I, (b) the predominant steady-state intermediates are in a rapid equilibrium between actin-bound and free states, (c) phosphate release is rate limiting and regulated by heavy-chain phosphorylation, and (d) ADP release is fast. Thus, during steady-state ATP hydrolysis, myosin-I is weakly bound to the actin filament like skeletal muscle myosin-II and unlike the microtubule-based motor kinesin. Therefore, for myosin-I to support processive motility or cortical contraction, multiple myosin-I molecules must be specifically localized to a small region on a membrane or in the actin-rich cell cortex. This conclusion has important implications for the regulation of myosin-I via localization through the unique myosin-I tails. This is the first complete transient kinetic characterization of a member of the myosin superfamily, other than myosin-II, providing the opportunity to obtain insights about the evolution of all myosin isoforms.
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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.