scholarly journals Actin Network Architecture Can Determine Myosin Motor Activity

Science ◽  
2012 ◽  
Vol 336 (6086) ◽  
pp. 1310-1314 ◽  
Author(s):  
A.-C. Reymann ◽  
R. Boujemaa-Paterski ◽  
J.-L. Martiel ◽  
C. Guerin ◽  
W. Cao ◽  
...  
Keyword(s):  
Motor Activity ◽  
Network Architecture ◽  
Actin Network ◽  
Myosin Motor

scholarly journals Spatial integration of mechanical forces by alpha-actinin establishes actin network symmetry

2019 ◽  
Author(s):  
Fabrice Senger ◽  
Amandine Pitaval ◽  
Hajer Ennomani ◽  
Laetitia Kurzawa ◽  
Laurent Blanchoin ◽  
...  
Keyword(s):  
Network Architecture ◽  
Spatial Organization ◽  
Global Network ◽  
Mechanical Forces ◽  
Spatial Integration ◽  
Actin Network ◽  
Entire Cell ◽  
Extracellular Microenvironment ◽  
Extracellular Environment

Cell and tissue morphogenesis depend on the production and spatial organization of tensional forces in the actin cytoskeleton. Actin network architecture is complex because it is made of distinct modules in which filaments adopt a variety of organizations. The assembly and dynamics of these modules is well described but the self-organisation rules directing the global network architecture are much less understood. Here we investigated the mechanism regulating the interplay between network architecture and the geometry of cell’s extracellular environment. We found that α-actinin, a filament crosslinker, is essential for network symmetry to be consistent with extracellular microenvironment symmetry. It appeared to be required for the interconnection of transverse arcs with radial fibres to ensure an appropriate balance between forces at cell adhesions and across the entire actin network. Furthermore, the connectivity of the actin network appeared necessary for the cell ability to integrate and adapt to complex patterns of extracellular cues as they migrate. Altogether, our study has unveiled a role of actin-filament crosslinking in the physical integration of mechanical forces throughout the entire cell, and the role of this integration in the establishment and adaptation of intracellular symmetry axes in accordance with the geometry of extracellular cues.

scholarly journals Myosin and gelsolin cooperate in actin filament severing and actomyosin motor activity

2020 ◽  
pp. jbc.RA120.015863
Author(s):  
Venukumar Vemula ◽  
Tamás Huber ◽  
Marko Ušaj ◽  
Beáta Bugyi ◽  
Alf Mansson
Keyword(s):  
Motor Activity ◽  
Actin Filament ◽  
Single Molecule ◽  
Actin Filaments ◽  
Actin Binding ◽  
In Vitro Motility Assay ◽  
Cooperative Effects ◽  
Myosin Motor ◽  
Filament Dynamics

Actin is a major intracellular protein with key functions in cellular motility, signaling and structural rearrangements. Its dynamic behavior, such as polymerisation and depolymerisation of actin filaments in response to intra- and extracellular cues, is regulated by an abundance of actin binding proteins. Out of these, gelsolin is one of the most potent for filament severing. However, myosin motor activity also fragments actin filaments through motor induced forces, suggesting that these two proteins could cooperate to regulate filament dynamics and motility. To test this idea, we used an in vitro motility assay, where actin filaments are propelled by surface-adsorbed heavy meromyosin (HMM) motor fragments. This allows studies of both motility and filament dynamics using isolated proteins. Gelsolin, at both nanomolar and micromolar Ca2+ concentration, appreciably enhanced actin filament severing caused by HMM-induced forces at 1 mM MgATP, an effect that was increased at higher HMM motor density. This finding is consistent with cooperativity between actin filament severing by myosin-induced forces and by gelsolin. We also observed reduced sliding velocity of the HMM-propelled filaments in the presence of gelsolin, providing further support of myosin-gelsolin cooperativity. Total internal reflection fluorescence microscopy based single molecule studies corroborated that the velocity reduction was a direct effect of gelsolin-binding to the filament and revealed different filament severing pattern of stationary and HMM propelled filaments. Overall, the results corroborate cooperative effects between gelsolin-induced alterations in the actin filaments and changes due to myosin motor activity leading to enhanced F-actin severing of possible physiological relevance.

scholarly journals Network Contractility during Cytokinesis—From Molecular to Global Views

Biomolecules ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 194 ◽  
Author(s):  
Joana Leite ◽  
Daniel Sampaio Osorio ◽  
Ana Filipa Sobral ◽  
Ana Marta Silva ◽  
Ana Xavier Carvalho
Keyword(s):  
Motor Activity ◽  
Network Architecture ◽  
Theoretical Models ◽  
Coarse Grained ◽  
Cell Cortex ◽  
Contractile Ring ◽  
Daughter Cells ◽  
Experimental Approaches ◽  
Global Understanding ◽  
Last Stage

Cytokinesis is the last stage of cell division, which partitions the mother cell into two daughter cells. It requires the assembly and constriction of a contractile ring that consists of a filamentous contractile network of actin and myosin. Network contractility depends on network architecture, level of connectivity and myosin motor activity, but how exactly is the contractile ring network organized or interconnected and how much it depends on motor activity remains unclear. Moreover, the contractile ring is not an isolated entity; rather, it is integrated into the surrounding cortex. Therefore, the mechanical properties of the cell cortex and cortical behaviors are expected to impact contractile ring functioning. Due to the complexity of the process, experimental approaches have been coupled to theoretical modeling in order to advance its global understanding. While earlier coarse-grained descriptions attempted to provide an integrated view of the process, recent models have mostly focused on understanding the behavior of an isolated contractile ring. Here we provide an overview of the organization and dynamics of the actomyosin network during cytokinesis and discuss existing theoretical models in light of cortical behaviors and experimental evidence from several systems. Our view on what is missing in current models and should be tested in the future is provided.

scholarly journals Filopod Extension Requires MyTH4-Ferm Myosin Motor Activity

2015 ◽  
Vol 108 (2) ◽  
pp. 303a
Author(s):  
Karl J. Petersen ◽  
G.W. Gant Luxton ◽  
Margaret A. Titus
Keyword(s):  
Motor Activity ◽  
Myosin Motor

scholarly journals Mechanism and Specificity of Pentachloropseudilin-mediated Inhibition of Myosin Motor Activity

2011 ◽  
Vol 286 (34) ◽  
pp. 29700-29708 ◽  
Author(s):  
Krishna Chinthalapudi ◽  
Manuel H. Taft ◽  
René Martin ◽  
Sarah M. Heissler ◽  
Matthias Preller ◽  
...  
Keyword(s):  
Motor Activity ◽  
Myosin Motor

Confinement Of Myosin Motor Activity On Trimethylchlorosilane Surface By Ultra Violet Light Exposure For Nano-Technology Applications

2008 ◽  
Vol 40 (Supplement) ◽  
pp. S297
Author(s):  
Madhukar B. Kolli ◽  
Hideyo Takatsuki ◽  
Devashish Desai ◽  
Kevin M. Rice ◽  
Sunil Kakarla ◽  
...  
Keyword(s):  
Motor Activity ◽  
Light Exposure ◽  
Ultra Violet ◽  
Nano Technology ◽  
Ultra Violet Light ◽  
Myosin Motor ◽  
Violet Light ◽  
Technology Applications

scholarly journals Structural basis for drug-induced allosteric changes to human β-cardiac myosin motor activity

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Donald A. Winkelmann ◽  
Eva Forgacs ◽  
Matthew T. Miller ◽  
Ann M. Stock
Keyword(s):  
Motor Activity ◽  
Structural Basis ◽  
Cardiac Myosin ◽  
Drug Induced ◽  
Myosin Motor

scholarly journals STAR syndrome-associated CDK10/Cyclin M regulates actin network architecture and ciliogenesis

Cell Cycle ◽  
2016 ◽  
Vol 15 (5) ◽  
pp. 678-688 ◽  
Author(s):  
Vincent J. Guen ◽  
Carly Gamble ◽  
Dahlia E. Perez ◽  
Sylvie Bourassa ◽  
Hildegard Zappel ◽  
...  
Keyword(s):  
Network Architecture ◽  
Actin Network
Sign in / Sign up

Export Citation Format

Share Document