ArticleThe Journal of biological chemistry2008
Load and Pi control flux through the branched kinetic cycle of myosin V.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 63 citations in OpenAlex.
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Information flow, gating, and energetics in dimeric molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cargo properties play a critical role in myosin Va-driven cargo transport along actin filaments.Biochemistry and biophysics reports · 2022Article
- Article
- A model for the chemomechanical coupling of myosin-V molecular motors.RSC advances · 2019Article
- Myosin Va transport of liposomes in three-dimensional actin networks is modulated by actin filament density, position, and polarity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Understanding the coupling between DNA damage detection and UvrA's ATPase using bulk and single molecule kinetics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- A Unified Walking Model for Dimeric Motor Proteins.Biophysical journal · 2018Article
- Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level.Nature communications · 2018Article
- Myosin V: Chemomechanical-coupling ratchet with load-induced mechanical slip.Scientific reports · 2017Article
- Reexamining the origin of the directionality of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Small teams of myosin Vc motors coordinate their stepping for efficient cargo transport on actin bundles.The Journal of biological chemistry · 2017Article
- Myosin Va molecular motors manoeuvre liposome cargo through suspended actin filament intersections in vitro.Nature communications · 2017Article
- Simulating the dynamics of the mechanochemical cycle of myosin-V.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Cargo Transport by Two Coupled Myosin Va Motors on Actin Filaments and Bundles.Biophysical journal · 2016Article
- Myosin Vc Is Specialized for Transport on a Secretory Superhighway.Current biology : CB · 2016Article
- Mechanochemical tuning of myosin-I by the N-terminal region.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Motor coupling through lipid membranes enhances transport velocities for ensembles of myosin Va.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Myosin V is a biological Brownian machine.Biophysics (Nagoya-shi, Japan) · 2014Review
- Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Myosin V is a processive actin-based motor protein that takes multiple 36-nm steps to deliver intracellular cargo to its destination. In the laser trap, applied load slows myosin V heavy meromyosin stepping and increases the probability of backsteps. In the presence of 40 mm phosphate (P(i)), both forward and backward steps become less load-dependent. From these data, we infer that P(i) release commits myosin V to undergo a highly load-dependent transition from a state in which ADP is bound to both heads and its lead head trapped in a pre-powerstroke conformation. Increasing the residence time in this state by applying load increases the probability of backstepping or detachment. The kinetics of detachment indicate that myosin V can detach from actin at two distinct points in the cycle, one of which is turned off by the presence of P(i). We propose a branched kinetic model to explain these data. Our model includes P(i) release prior to the most load-dependent step in the cycle, implying that P(i) release and load both act as checkpoints that control the flux through two parallel pathways.
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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.