Interactions between Myosin and Actin Crosslinkers Control Cytokinesis Contractility Dynamics and Mechanics

Reichl, Elizabeth M.; Ren, Yixin; Morphew, Mary K.; Delannoy, Michaël; Effler, Janet C.; Girard, Kristine D.; Divi, Srikanth; Iglesias, Pablo A.; Kuo, Scot C.; Robinson, Douglas N.

doi:10.1016/j.cub.2008.02.056

Cited by 164 publications

(250 citation statements)

References 48 publications

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“…Our data add another layer to our understanding of the function of myosin II in exocytosis. By maintaining tension of the cortical actin network 18,19,40 in unstimulated cells, myosin II retains most SVs away from the plasma membrane. This is in good agreement with previous reports showing that the cortical actin network acts as a barrier, preventing the majority of vesicles from accessing the plasma membrane in resting conditions 2,9 .…”

Section: Discussionmentioning

confidence: 99%

Activity-driven relaxation of the cortical actomyosin II network synchronizes Munc18-1-dependent neurosecretory vesicle docking

et al. 2015

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In neurosecretory cells, secretory vesicles (SVs) undergo Ca 2 þ -dependent fusion with the plasma membrane to release neurotransmitters. How SVs cross the dense mesh of the cortical actin network to reach the plasma membrane remains unclear. Here we reveal that, in bovine chromaffin cells, SVs embedded in the cortical actin network undergo a highly synchronized transition towards the plasma membrane and Munc18-1-dependent docking in response to secretagogues. This movement coincides with a translocation of the cortical actin network in the same direction. Both effects are abolished by the knockdown or the pharmacological inhibition of myosin II, suggesting changes in actomyosin-generated forces across the cell cortex. Indeed, we report a reduction in cortical actin network tension elicited on secretagogue stimulation that is sensitive to myosin II inhibition. We reveal that the cortical actin network acts as a 'casting net' that undergoes activity-dependent relaxation, thereby driving tethered SVs towards the plasma membrane where they undergo Munc18-1-dependent docking.

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Section: Discussionmentioning

confidence: 99%

Activity-driven relaxation of the cortical actomyosin II network synchronizes Munc18-1-dependent neurosecretory vesicle docking

et al. 2015

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“…First, as the furrow ingresses, resistive stresses can build in the two daughter cell cortices and cytoplasm, slowing furrow ingression. Genetic mutants devoid of myosin II, key actin cross-linkers, or cytoskeletal regulators that control the polar cortices appear to alleviate this resistive stress (4). Second, the accumulation of the cytokinetic machinery, including myosin II and actin cross-linkers, to the cleavage furrow cortex can lead to strain stiffening of the cytoskeletal network, making it more difficult for the cortex network to remodel (making it more elastic) (19,22).…”

Section: Forces Acting On the Cell Cortexmentioning

confidence: 99%

“…The cortex contains structural proteins that exhibit distinct physical properties and kinetics of binding and detachment, and are poised to respond dynamically to chemical and mechanical signals to effect shape changes. The cortex is comprised of actin filaments organized in a meshwork~200 nm thick (3,4), cross-linked by actincross-linking proteins and nonmuscle myosin IIs, which are the primary drivers of network contraction in cells. Among these structural elements are regulatory proteins that control actin and myosin dynamics, factors that regulate protein turnover, membrane linkers, scaffolding/adaptor proteins, Rho GTPases, Rho GTPase effectors, and Rho GAPs/GEFs (5).…”

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confidence: 99%

“…Among these structural elements are regulatory proteins that control actin and myosin dynamics, factors that regulate protein turnover, membrane linkers, scaffolding/adaptor proteins, Rho GTPases, Rho GTPase effectors, and Rho GAPs/GEFs (5). The actin filaments in the cortex are quite short: in the social amoeba Dictyostelium, the average actin filament length is~100 nm (4,6). In mammalian cells, identifying a characteristic length is more challenging because of cell-type diversity, but for leukocytes it is~300 nm, with the majority being <180 nm in length (7), slightly longer than in Dictyostelium.…”

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confidence: 99%

“…Furthermore, in cells, active processes that require ATP hydrolysis can also stir these elements, promoting the emergence of a viscous-like character (11,12). Cell-cortex mechanics at these scales have been analyzed in Dictyostelium (4,13,14) and in multiple mammalian cell types (15,16). In these low-force regimes, cells are predominantly elastic with a mechanical phase angle of~10-15 .…”

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confidence: 99%

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Mechanochemical Signaling Directs Cell-Shape Change

Schiffhauer

Robinson

2017

Biophysical Journal

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For specialized cell function, as well as active cell behaviors such as division, migration, and tissue development, cells must undergo dynamic changes in shape. To complete these processes, cells integrate chemical and mechanical signals to direct force production. This mechanochemical integration allows for the rapid production and adaptation of leading-edge machinery in migrating cells, the invasion of one cell into another during cell-cell fusion, and the force-feedback loops that ensure robust cytokinesis. A quantitative understanding of cell mechanics coupled with protein dynamics has allowed us to account for furrow ingression during cytokinesis, a model cell-shape-change process. At the core of cell-shape changes is the ability of the cell's machinery to sense mechanical forces and tune the force-generating machinery as needed. Force-sensitive cytoskeletal proteins, including myosin II motors and actin cross-linkers such as a-actinin and filamin, accumulate in response to internally generated and externally imposed mechanical stresses, endowing the cell with the ability to discern and respond to mechanical cues. The physical theory behind how these proteins display mechanosensitive accumulation has allowed us to predict paralogspecific behaviors of different cross-linking proteins and identify a zone of optimal actin-binding affinity that allows for mechanical stress-induced protein accumulation. These molecular mechanisms coupled with the mechanical feedback systems ensure robust shape changes, but if they go awry, they are poised to promote disease states such as cancer cell metastasis and loss of tissue integrity.The concept ''form begets function begets form'' provides an excellent foundation for understanding the behavior of biological systems. Even specialized cells, the smallest unit of complex living systems, perform all of the necessary functions of an organism by assuming distinct shapes, mechanical properties, and physical behaviors. Different cell types use a common set of cytoskeletal elements to provide precise physical support for their distinct functions. For example, red blood cells and neurons have very different shapes that allow them to perform their specific roles. However, they both utilize alternating patterns of actin and spectrin to form cortices with appropriate viscous and elastic properties, albeit in different structural arrangements. Perturbations to this structural network cause a breakdown in the mechanical properties, or the form, of these cells, which inhibits cell function (1,2).Fascinatingly, the physical properties of cells are both determined and acted upon by the cytoskeletal apparatus. Cells are capable of modifying their own physical properties and driving changes in cell shape in response to internal and external chemical and mechanical stimuli. These modifications occur through the remodeling of the cell cortex, the network of cytoskeletal proteins directly under the plasma membrane. Much progress has been made recently in deciphering how chemical signa...

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Simulating Filament Dynamics in Cellular Systems

Channels

Iglesias

2010

Elements of Computational Systems Biology

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Interactions between Myosin and Actin Crosslinkers Control Cytokinesis Contractility Dynamics and Mechanics

Cited by 164 publications

References 48 publications

Activity-driven relaxation of the cortical actomyosin II network synchronizes Munc18-1-dependent neurosecretory vesicle docking

Activity-driven relaxation of the cortical actomyosin II network synchronizes Munc18-1-dependent neurosecretory vesicle docking

Mechanochemical Signaling Directs Cell-Shape Change

Simulating Filament Dynamics in Cellular Systems

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