Tuning molecular motor transport through cytoskeletal filament network organization

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.

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Tuning molecular motor transport through cytoskeletal filament network organization

Soft Matter ◽

10.1039/c9sm01904a ◽

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.

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Contribution of Filopodia to Cell Migration: A Mechanical Link between Protrusion and Contraction

International Journal of Cell Biology ◽

10.1155/2010/507821 ◽

2010 ◽

Vol 2010 ◽

pp. 1-13 ◽

Cited By ~ 31

Author(s):

Fei Xue ◽

Deanna M. Janzen ◽

David A. Knecht

Keyword(s):

Cell Migration ◽

Actin Polymerization ◽

Myosin Ii ◽

Temporal Distribution ◽

Leading Edge ◽

Distal Portion ◽

Actin Binding ◽

Actin Networks ◽

Motile Cells ◽

A Cell

Numerous F-actin containing structures are involved in regulating protrusion of membrane at the leading edge of motile cells. We have investigated the structure and dynamics of filopodia as they relate to events at the leading edge and the function of the trailing actin networks. We have found that although filopodia contain parallel bundles of actin, they contain a surprisingly nonuniform spatial and temporal distribution of actin binding proteins. Along the length of the actin filaments in a single filopodium, the most distal portion contains primarily T-plastin, while the proximal portion is primarily bound byα-actinin and coronin. Some filopodia are stationary, but lateral filopodia move with respect to the leading edge. They appear to form a mechanical link between the actin polymerization network at the front of the cell and the myosin motor activity in the cell body. The direction of lateral filopodial movement is associated with the direction of cell migration. When lateral filopodia initiate from and move toward only one side of a cell, the cell will turn opposite to the direction of filopodial flow. Therefore, this filopodia-myosin II system allows actin polymerization driven protrusion forces and myosin II mediated contractile force to be mechanically coordinated.

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Molecular Motor Proteins of the Kinesin Superfamily Proteins (KIFs): Structure, Cargo and Disease

Journal of Korean Medical Science ◽

10.3346/jkms.2004.19.1.1 ◽

2004 ◽

Vol 19 (1) ◽

pp. 1 ◽

Cited By ~ 26

Author(s):

Dae-Hyun Seog ◽

Dae-Ho Lee ◽

Sang-Kyoung Lee

Keyword(s):

Motor Proteins ◽

Molecular Motor ◽

Kinesin Superfamily

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

Physiology ◽

10.1152/nips.01389.2002 ◽

2002 ◽

Vol 17 (5) ◽

pp. 213-218 ◽

Cited By ~ 3

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.

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1P151 Athermal Fluctuations of Probe Particles in Active Cytoskeletal Networks(11.Molecular motor,Poster,The 51st Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri ◽

10.2142/biophys.53.s130_6 ◽

2013 ◽

Vol 53 (supplement1-2) ◽

pp. S130

Author(s):

Irwin Zaid ◽

Heev Ayade ◽

Julia Yeomans ◽

Daisuke Mizuno

Keyword(s):

Annual Meeting ◽

Molecular Motor ◽

Biophysical Society ◽

Cytoskeletal Networks ◽

Probe Particles

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Tensins – emerging insights into their domain functions, biological roles and disease relevance

Journal of Cell Science ◽

10.1242/jcs.254029 ◽

2021 ◽

Vol 134 (4) ◽

pp. jcs254029

Author(s):

Yi-Chun Liao ◽

Su Hao Lo

Keyword(s):

Focal Adhesion ◽

Muscle Regeneration ◽

Normal Tissue ◽

Physiological Processes ◽

Focal Adhesion Proteins ◽

A Cell ◽

Disease Relevance ◽

Cytoskeletal Networks ◽

Multiple Domains ◽

Mechanical Sensing

ABSTRACTTensins are a family of focal adhesion proteins consisting of four members in mammals (TNS1, TNS2, TNS3 and TNS4). Their multiple domains and activities contribute to the molecular linkage between the extracellular matrix and cytoskeletal networks, as well as mediating signal transduction pathways, leading to a variety of physiological processes, including cell proliferation, attachment, migration and mechanical sensing in a cell. Tensins are required for maintaining normal tissue structures and functions, especially in the kidney and heart, as well as in muscle regeneration, in animals. This Review discusses our current understanding of the domain functions and biological roles of tensins in cells and mice, as well as highlighting their relevance to human diseases.

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Mechanical bistability enabled by ectodermal compression facilitates Drosophila mesoderm invagination

10.1101/2021.03.18.435928 ◽

2021 ◽

Author(s):

Hanqing Guo ◽

Michael Swan ◽

Shicheng Huang ◽

Bing He

Keyword(s):

Myosin Ii ◽

Cell Sheet ◽

Apical Surface ◽

Apical Constriction ◽

Out Of Plane ◽

A Cell ◽

Plane Compression ◽

Contractile Forces ◽

Tissue Relaxation ◽

Muscle Myosin

Apical constriction driven by non-muscle myosin II (″myosin″) provides a well-conserved mechanism to mediate epithelial folding. It remains unclear how contractile forces near the apical surface of a cell sheet drive out-of-plane bending of the sheet and whether myosin contractility is required throughout folding. By optogenetic-mediated acute inhibition of myosin, we find that during Drosophila mesoderm invagination, myosin contractility is critical to prevent tissue relaxation during the early, ″priming″ stage of folding but is dispensable for the actual folding step after the tissue passes through a stereotyped transitional configuration, suggesting that the mesoderm is mechanically bistable during gastrulation. Combining computer modeling and experimental measurements, we show that the observed mechanical bistability arises from an in-plane compression from the surrounding ectoderm, which promotes mesoderm invagination by facilitating a buckling transition. Our results indicate that Drosophila mesoderm invagination requires a joint action of local apical constriction and global in-plane compression to trigger epithelial buckling.

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

Cells ◽

10.3390/cells9061458 ◽

2020 ◽

Vol 9 (6) ◽

pp. 1458 ◽

Cited By ~ 2

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.

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