scholarly journals Tuning molecular motor transport through cytoskeletal filament network organization

Soft Matter ◽  
2020 ◽  
Vol 16 (8) ◽  
pp. 2135-2140
Author(s):  
Monika Scholz ◽  
Kimberly L. Weirich ◽  
Margaret L. Gardel ◽  
Aaron R. Dinner
Keyword(s):  
Molecular Motor ◽  
Myosin Ii ◽  
Network Organization ◽  
Motor Transport ◽  
Cytoskeletal Filament ◽  
Underlying Network ◽  
Filament Network ◽  
Motor Dynamics

Myosin II motor dynamics have signatures that report on the structure of the underlying network of crosslinked cytoskeletal filaments.

scholarly journals Tuning molecular motor transport through cytoskeletal filament network organization

2018 ◽  
Author(s):  
Monika Scholz ◽  
Kimberly L. Weirich ◽  
Margaret L. Gardel ◽  
Aaron R. Dinner
Keyword(s):  
Motor Proteins ◽  
Molecular Motor ◽  
Myosin Ii ◽  
Transport Processes ◽  
Force Generation ◽  
Transport Dynamics ◽  
Cytoskeletal Filament ◽  
A Cell ◽  
Cytoskeletal Networks ◽  
Filament Network

The interaction of motor proteins with intracellular filaments is required for transport processes and force generation in cells. Within a cell, crosslinking proteins organize cytoskeletal filaments both temporally and spatially to create dynamic, and structurally diverse networks. The architecture of these networks changes both the mechanics as well as the transport dynamics; however, the effects on transport are less well understood. Here, we compare the transport dynamics of myosin II motor proteins moving on model cytoskeletal networks created by common crosslinking proteins. We observe that motor dynamics change predictably based on the microstructure of the underlying networks and discuss how this can be utilized by cells to achieve specific transport goals.

Molecular Motors: Force and Movement Generated by Single Myosin II Molecules

Physiology ◽  
2002 ◽  
Vol 17 (5) ◽  
pp. 213-218 ◽  
Author(s):  
Caspar Rüegg ◽  
Claudia Veigel ◽  
Justin E. Molloy ◽  
Stephan Schmitz ◽  
John C. Sparrow ◽  
...  
Keyword(s):  
Optical Tweezers ◽  
Single Molecule ◽  
Molecular Motors ◽  
Molecular Motor ◽  
Myosin Ii ◽  
Force Production ◽  
Myosin Isoforms ◽  
Single Molecule Level ◽  
Recent Developments ◽  
Muscle Myosin

Muscle myosin II is an ATP-driven, actin-based molecular motor. Recent developments in optical tweezers technology have made it possible to study movement and force production on the single-molecule level and to find out how different myosin isoforms may have adapted to their specific physiological roles.

Collective Molecular Motor Transport

2021 ◽  
pp. 195-208
Author(s):  
Christopher Miles ◽  
Alex Mogilner
Keyword(s):  
Molecular Motor ◽  
Motor Transport

scholarly journals Linking the Landscape of MYH9-Related Diseases to the Molecular Mechanisms that Control Non-Muscle Myosin II-A Function in Cells

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1458 ◽  
Author(s):  
Gloria Asensio-Juárez ◽  
Clara Llorente-González ◽  
Miguel Vicente-Manzanares
Keyword(s):  
Molecular Mechanisms ◽  
Clinical Presentation ◽  
Molecular Motor ◽  
Myosin Ii ◽  
Residual Activity ◽  
Cellular Level ◽  
Actin Binding ◽  
Compensatory Mechanisms ◽  
Myh9 Gene ◽  
Muscle Myosin

The MYH9 gene encodes the heavy chain (MHCII) of non-muscle myosin II A (NMII-A). This is an actin-binding molecular motor essential for development that participates in many crucial cellular processes such as adhesion, cell migration, cytokinesis and polarization, maintenance of cell shape and signal transduction. Several types of mutations in the MYH9 gene cause an array of autosomal dominant disorders, globally known as MYH9-related diseases (MYH9-RD). These include May-Hegglin anomaly (MHA), Epstein syndrome (EPS), Fechtner syndrome (FTS) and Sebastian platelet syndrome (SPS). Although caused by different MYH9 mutations, all patients present macrothrombocytopenia, but may later display other pathologies, including loss of hearing, renal failure and presenile cataracts. The correlation between the molecular and cellular effects of the different mutations and clinical presentation are beginning to be established. In this review, we correlate the defects that MYH9 mutations cause at a molecular and cellular level (for example, deficient filament formation, altered ATPase activity or actin-binding) with the clinical presentation of the syndromes in human patients. We address why these syndromes are tissue restricted, and the existence of possible compensatory mechanisms, including residual activity of mutant NMII-A and/or the formation of heteropolymers or co-polymers with other NMII isoforms.

scholarly journals Mechanical parameters of the molecular motor myosin II determined in permeabilised fibres from slow and fast skeletal muscles of the rabbit

2018 ◽  
Vol 596 (7) ◽  
pp. 1243-1257 ◽  
Author(s):  
Valentina Percario ◽  
Simona Boncompagni ◽  
Feliciano Protasi ◽  
Irene Pertici ◽  
Francesca Pinzauti ◽  
...  
Keyword(s):  
Skeletal Muscles ◽  
Molecular Motor ◽  
Myosin Ii ◽  
Mechanical Parameters

A Dynamic Escape Problem of Molecular Motors

2020 ◽  
Vol 142 (5) ◽  
Author(s):  
Dean Culver ◽  
Bryan Glaz ◽  
Samuel Stanton
Keyword(s):  
Molecular Motors ◽  
Binding Sites ◽  
Molecular Motor ◽  
Myosin Ii ◽  
Three Dimensional ◽  
Production Capacity ◽  
Force Production ◽  
Actin Binding ◽  
Three Dimensional Model ◽  
Thermal Agitation

Abstract Animal skeletal muscle exhibits very interesting behavior at near-stall forces (when the muscle is loaded so strongly that it can barely contract). Near this physical limit, the myosin II proteins may be unable to reach advantageous actin binding sites through simple attractive forces. It has been shown that the advantageous utilization of thermal agitation is a likely source for an increased force-production capacity and reach in myosin-V (a processing motor protein), and here we explore the dynamics of a molecular motor without hand-over-hand motion including Brownian motion to show how local elastic energy well boundaries may be overcome. We revisit a spatially two-dimensional mechanical model to illustrate how thermal agitation can be harvested for useful mechanical work in molecular machinery inspired by this biomechanical phenomenon without rate functions or empirically inspired spatial potential functions. Additionally, the model accommodates variable lattice spacing, and it paves the way for a full three-dimensional model of cross-bridge interactions where myosin II may be azimuthally misaligned with actin binding sites. With potential energy sources based entirely on realizable components, this model lends itself to the design of artificial, molecular-scale motors.

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