Actin cortex mechanics and cellular morphogenesis

Salbreux, Guillaume; Charras, Guillaume; Paluch, Ewa K.

doi:10.1016/j.tcb.2012.07.001

Cited by 764 publications

(891 citation statements)

References 108 publications

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“…The area underneath the plasma membrane, the cortex, is a particularly prominent site of actin dynamics, supporting essential mechanical functions of the cell (Fig 1) 11 .…”

Section: [H1] Structure Of the Cortical Cytoskeletonmentioning

confidence: 98%

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Cytoskeletal control of B cell responses to antigens

Tolar

2017

Nat Rev Immunol

122

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The actin cytoskeleton is essential for cell mechanics and has increasingly been implicated in the regulation of cell signalling. In B cells, the actin cytoskeleton couples extensively to B cell receptor (BCR) signalling pathways and its defects can either enhance or suppress B cell activation. Recent insights from single-cell imaging and biophysical techniques suggest that actin orchestrates BCR signalling at the plasma membrane through effects on protein diffusion, and that it regulates antigen discrimination through the biomechanics of immune synapses. These mechanical functions also play a role in the adaptation of B cell subsets to specialized tasks during antibody responses.3

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“…The area underneath the plasma membrane, the cortex, is a particularly prominent site of actin dynamics, supporting essential mechanical functions of the cell (Fig 1) 11 .…”

Section: [H1] Structure Of the Cortical Cytoskeletonmentioning

confidence: 98%

“…In addition to pushing on the membrane, the cortex also generates tension 11 . The tension is produced by class II myosins, represented in lymphocytes by myosin IIa.…”

Section: [H1] Structure Of the Cortical Cytoskeletonmentioning

confidence: 99%

Cytoskeletal control of B cell responses to antigens

Tolar

2017

Nat Rev Immunol

122

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“…To study the effect of membrane tension and back pressure from the cytosol, we consider an extreme case in which the cell translocates almost all cytosol before nuclear transmigration, meaning that r r zr n and r f ¼ 2:5r n , which is commonly seen in our experiments with very small gap sizes. To estimate the pressure difference, we consider a cortical actin tension of g ¼ 2 Â 10 À3 J=m 2 based on a previous study (35). The additional driving force due to cytosolic pressure is DF ¼ Dppr 02 g , where r 0 g is the endothelial gap radius in the current state (Fig.…”

Section: Contribution Of Cytosolic Back Pressure To Transmigrationmentioning

confidence: 99%

A Chemomechanical Model for Nuclear Morphology and Stresses during Cell Transendothelial Migration

Cao

Moeendarbary

Isermann

et al. 2016

Biophysical Journal

116

160

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It is now evident that the cell nucleus undergoes dramatic shape changes during important cellular processes such as cell transmigration through extracellular matrix and endothelium. Recent experimental data suggest that during cell transmigration the deformability of the nucleus could be a limiting factor, and the morphological and structural alterations that the nucleus encounters can perturb genomic organization that in turn influences cellular behavior. Despite its importance, a biophysical model that connects the experimentally observed nuclear morphological changes to the underlying biophysical factors during transmigration through small constrictions is still lacking. Here, we developed a universal chemomechanical model that describes nuclear strains and shapes and predicts thresholds for the rupture of the nuclear envelope and for nuclear plastic deformation during transmigration through small constrictions. The model includes actin contraction and cytosolic back pressure that squeeze the nucleus through constrictions and overcome the mechanical resistance from deformation of the nucleus and the constrictions. The nucleus is treated as an elastic shell encompassing a poroelastic material representing the nuclear envelope and inner nucleoplasm, respectively. Tuning the chemomechanical parameters of different components such as cell contractility and nuclear and matrix stiffnesses, our model predicts the lower bounds of constriction size for successful transmigration. Furthermore, treating the chromatin as a plastic material, our model faithfully reproduced the experimentally observed irreversible nuclear deformations after transmigration in lamin-A/C-deficient cells, whereas the wild-type cells show much less plastic deformation. Along with making testable predictions, which are in accord with our experiments and existing literature, our work provides a realistic framework to assess the biophysical modulators of nuclear deformation during cell transmigration.

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“…SVs can be tethered to the cortical actin network by myosin VI in an activity-dependent manner 10 , and can also be transported along actin fibres by myosin Va 11 . Recent work has also highlighted a role for myosin II in exocytosis [12][13][14][15][16][17] , as well as demonstrating its ability to maintain the cortical actin network under tension [18][19][20] . How these molecular motors act to direct SVs towards their docking sites remains unclear.…”

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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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Actin cortex mechanics and cellular morphogenesis

Cited by 764 publications

References 108 publications

Cytoskeletal control of B cell responses to antigens

Cytoskeletal control of B cell responses to antigens

A Chemomechanical Model for Nuclear Morphology and Stresses during Cell Transendothelial Migration

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

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