scholarly journals A model for the chemomechanical coupling of myosin-V molecular motors

RSC Advances ◽  
2019 ◽  
Vol 9 (46) ◽  
pp. 26734-26747 ◽  
Author(s):  
Ping Xie
Keyword(s):  
Molecular Motors ◽  
Myosin V ◽  
Chemomechanical Coupling

The paper presents a model of chemomechanical coupling of myosin-V motor, explaining the dynamics under varying force and ATP concentrations.

A non-tight chemomechanical coupling model for force-dependence of movement dynamics of molecular motors

2018 ◽  
Vol 20 (7) ◽  
pp. 4752-4759 ◽  
Author(s):  
Ping Xie ◽  
Hong Chen
Keyword(s):  
Experimental Data ◽  
Single Molecule ◽  
Molecular Motors ◽  
General Model ◽  
Coupling Model ◽  
Myosin V ◽  
Chemomechanical Coupling ◽  
Movement Dynamics

We present a simple yet general model that can quantitatively reproduce diverse single-molecule experimental data on dimeric kinesin and myosin-V.

scholarly journals A model of processive walking and slipping of kinesin-8 molecular motors

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ping Xie
Keyword(s):  
Single Molecule ◽  
Molecular Motors ◽  
External Load ◽  
Molecular Motor ◽  
Velocity Versus ◽  
Stick Slip ◽  
Load Dependence ◽  
Chemomechanical Coupling ◽  
Similarities And Differences ◽  
Stick Slip Motion

AbstractKinesin-8 molecular motor can move with superprocessivity on microtubules towards the plus end by hydrolyzing ATP molecules, depolymerizing microtubules. The available single molecule data for yeast kinesin-8 (Kip3) motor showed that its superprocessive movement is frequently interrupted by brief stick–slip motion. Here, a model is presented for the chemomechanical coupling of the kinesin-8 motor. On the basis of the model, the dynamics of Kip3 motor is studied analytically. The analytical results reproduce quantitatively the available single molecule data on velocity without including the slip and that with including the slip versus external load at saturating ATP as well as slipping velocity versus external load at saturating ADP and no ATP. Predicted results on load dependence of stepping ratio at saturating ATP and load dependence of velocity at non-saturating ATP are provided. Similarities and differences between dynamics of kinesin-8 and that of kinesin-1 are discussed.

scholarly journals 2P130 Dynamic cooperative binding of myosin V on actin filament(Molecular motors,Poster Presentations)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S145
Author(s):  
Jun Kozuka ◽  
Yoshiharu Ishii ◽  
Toshio Yanagida
Keyword(s):  
Actin Filament ◽  
Molecular Motors ◽  
Cooperative Binding ◽  
Myosin V ◽  
Poster Presentations

scholarly journals The novel proteins Rng8 and Rng9 regulate the myosin-V Myo51 during fission yeast cytokinesis

2014 ◽  
Vol 205 (3) ◽  
pp. 357-375 ◽  
Author(s):  
Ning Wang ◽  
Libera Lo Presti ◽  
Yi-Hua Zhu ◽  
Minhee Kang ◽  
Zhengrong Wu ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Molecular Motors ◽  
Coiled Coil ◽  
Myosin V ◽  
Contractile Ring ◽  
Novel Proteins ◽  
Ring Assembly ◽  
Actin Cables ◽  
Order Complexes

The myosin-V family of molecular motors is known to be under sophisticated regulation, but our knowledge of the roles and regulation of myosin-Vs in cytokinesis is limited. Here, we report that the myosin-V Myo51 affects contractile ring assembly and stability during fission yeast cytokinesis, and is regulated by two novel coiled-coil proteins, Rng8 and Rng9. Both rng8Δ and rng9Δ cells display similar defects as myo51Δ in cytokinesis. Rng8 and Rng9 are required for Myo51’s localizations to cytoplasmic puncta, actin cables, and the contractile ring. Myo51 puncta contain multiple Myo51 molecules and walk continuously on actin filaments in rng8+ cells, whereas Myo51 forms speckles containing only one dimer and does not move efficiently on actin tracks in rng8Δ. Consistently, Myo51 transports artificial cargos efficiently in vivo, and this activity is regulated by Rng8. Purified Rng8 and Rng9 form stable higher-order complexes. Collectively, we propose that Rng8 and Rng9 form oligomers and cluster multiple Myo51 dimers to regulate Myo51 localization and functions.

scholarly journals Cluster models of molecular motors: kinesin and myosin V

2014 ◽  
Vol 6 (5) ◽  
pp. 747-760
Author(s):  
V. P. Trifonenkov ◽  
A. V. Kargovsky
Keyword(s):  
Molecular Motors ◽  
Cluster Models ◽  
Myosin V

scholarly journals A Generalized Kinetic Model for Coupling between Stepping and ATP Hydrolysis of Kinesin Molecular Motors

2019 ◽  
Vol 20 (19) ◽  
pp. 4911 ◽  
Author(s):  
Xie ◽  
Guo ◽  
Chen
Keyword(s):  
Kinetic Model ◽  
Atpase Activity ◽  
Single Molecule ◽  
Rate Constants ◽  
Molecular Motors ◽  
Atp Hydrolysis ◽  
Power Production ◽  
Wild Type ◽  
Chemomechanical Coupling ◽  
Generalized Kinetic Model

A general kinetic model is presented for the chemomechanical coupling of dimeric kinesin molecular motors with and without extension of their neck linkers (NLs). A peculiar feature of the model is that the rate constants of ATPase activity of a kinesin head are independent of the strain on its NL, implying that the heads of the wild-type kinesin dimer and the mutant with extension of its NLs have the same force-independent rate constants of the ATPase activity. Based on the model, an analytical theory is presented on the force dependence of the dynamics of kinesin dimers with and without extension of their NLs at saturating ATP. With only a few adjustable parameters, diverse available single molecule data on the dynamics of various kinesin dimers, such as wild-type kinesin-1, kinesin-1 with mutated residues in the NLs, kinesin-1 with extension of the NLs and wild-type kinesin-2, under varying force and ATP concentration, can be reproduced very well. Additionally, we compare the power production among different kinesin dimers, showing that the mutation in the NLs reduces the power production and the extension of the NLs further reduces the power production.

scholarly journals 2P133 Actin gliding over myosin V S1 tethered on a glass surface at the head domain(Molecular motors,Oral Presentations)

2007 ◽  
Vol 47 (supplement) ◽  
pp. S146
Author(s):  
Naoki Nagura ◽  
Yuta Saito ◽  
Yusuke Tanaka ◽  
Toshio Ando
Keyword(s):  
Molecular Motors ◽  
Glass Surface ◽  
Myosin V ◽  
Head Domain ◽  
Oral Presentations

scholarly journals Secretory vesicle transport velocity in living cells depends on the myosin-V lever arm length

2002 ◽  
Vol 156 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Daniel H. Schott ◽  
Ruth N. Collins ◽  
Anthony Bretscher
Keyword(s):  
Molecular Motors ◽  
Secretory Vesicle ◽  
Genetically Engineered ◽  
Secretory Vesicles ◽  
Myosin V ◽  
Lever Arm ◽  
Wide Range ◽  
Transport Velocity ◽  
Maximal Speed ◽  
Muscle Myosin

Myosins are molecular motors that exert force against actin filaments. One widely conserved myosin class, the myosin-Vs, recruits organelles to polarized sites in animal and fungal cells. However, it has been unclear whether myosin-Vs actively transport organelles, and whether the recently challenged lever arm model developed for muscle myosin applies to myosin-Vs. Here we demonstrate in living, intact yeast that secretory vesicles move rapidly toward their site of exocytosis. The maximal speed varies linearly over a wide range of lever arm lengths genetically engineered into the myosin-V heavy chain encoded by the MYO2 gene. Thus, secretory vesicle polarization is achieved through active transport by a myosin-V, and the motor mechanism is consistent with the lever arm model.

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