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Related Concept Videos

Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
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Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶  nucleation, elongation, and steady-state phase.
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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across...
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Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
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The Mechanics of Poro-Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
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Actin-myosin spatial patterns from a simplified isotropic viscoelastic model.

Owen L Lewis1, Robert D Guy1, Jun F Allard2

  • 1Department of Mathematics, University of California at Davis, Davis, California.

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|August 21, 2014
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Summary

This study models F-actin networks, revealing how slow reorganization and disassembly create spherical shells. These findings explain complex F-actin patterns without external spatial cues.

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Area of Science:

  • Cell biology
  • Biophysics
  • Materials science

Background:

  • F-actin networks are crucial for cellular mechanics like motility and endocytosis.
  • The mesoscale architecture and micrometer-scale rheological properties of F-actin assemblies are not well understood.
  • In vitro F-actin networks can form spatial patterns, such as spherical shells, when confined.

Purpose of the Study:

  • To model the self-organization of F-actin networks.
  • To understand the emergence of spatial patterns, specifically spherical shells, in F-actin assemblies.
  • To elucidate the relationship between network dynamics and pattern formation.

Main Methods:

  • Development of a simplified model for an isotropic, compressible, viscoelastic material with continuous assembly and disassembly.
  • Simulation of F-actin network behavior under confinement.
  • Analysis of pattern formation based on strain relaxation and disassembly rates.

Main Results:

  • Spherical shells of F-actin naturally emerge when the strain relaxation rate is slower than the disassembly rate.
  • These simulated patterns are consistent with experimental observations of F-actin shells in emulsion droplets.
  • Drug-induced changes in assembly or disassembly rates lead to shell collapse into a central F-actin focus.

Conclusions:

  • Complex spatio-temporal patterns in F-actin networks can arise from intrinsic material properties and dynamics.
  • Emergence of spherical shells does not require spatially distributed force generation or polar alignment.
  • The model provides a framework for understanding how F-actin mesoscale architecture influences cellular mechanical processes.