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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.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
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Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Actin Treadmilling01:18

Actin Treadmilling

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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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Related Experiment Video

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Reconstitution of Actin-Based Motility with Commercially Available Proteins

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Control of actin-based motility through localized actin binding.

Edward J Banigan1, Kun-Chun Lee, Andrea J Liu

  • 1Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA 19104, USA.

Physical Biology
|November 15, 2013
PubMed
Summary

Actin polymerization propels objects by creating a concentration gradient, even with binding interactions. This model explains how actin tails drive motility and network growth against external loads.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Biomimetic Systems

Background:

  • Actin polymerization drives motility in various biological and biomimetic systems.
  • Propulsion mechanisms require both actin binding and repulsion, posing a key question about their interplay.

Purpose of the Study:

  • To develop a physically consistent model for actin-based motility.
  • To investigate how attractive and repulsive interactions between actin and an object influence propulsion.

Main Methods:

  • Brownian dynamics modeling incorporating the dendritic nucleation model.
  • Simulation of interactions between filamentous actin and a moveable disc.

Main Results:

  • A concentration gradient of filamentous actin is sufficient for propulsion, even with moderate binding.
  • Actin binding can modulate network growth and act as a biophysical cap.
  • The model predicts motility against loads up to a stall pressure dependent on actin network properties.

Conclusions:

  • The developed model provides a robust explanation for actin-based motility.
  • It reconciles the roles of actin binding and repulsion in object propulsion.
  • The findings offer insights into controlling motility through network dynamics.