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Actin Filament Depolymerization

Actin Filament Depolymerization

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...

Generation of Straight or Branched Actin Filaments

Generation of Straight or Branched Actin Filaments

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...

Actin Polymerization

Actin Polymerization

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.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...

Disassembly of Intermediate Filaments

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...

Mechanism of Filopodia Formation

Mechanism of Filopodia Formation

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...

Actin Treadmilling

Actin Treadmilling

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

Updated: May 13, 2026

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Actin depolymerization under force is governed by lysine 113:glutamic acid 195-mediated catch-slip bonds.

Cho-yin Lee¹, Jizhong Lou, Kuo-kuang Wen

¹Wallace H. Coulter Department of Biomedical Engineering, Georgia Institute of Technology, Atlanta, GA 30332, USA.

Proceedings of the National Academy of Sciences of the United States of America

|March 6, 2013

Summary

Tensile force regulates actin filament dynamics through catch-slip bonds. This mechanism involves specific protein interactions, offering insights into how cells manage cytoskeletal forces.

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Area of Science:

Biophysics
Cell Biology
Structural Biology

Background:

Actin filaments are crucial cytoskeletal components that undergo constant force-induced dynamics.
The precise mechanisms by which external forces regulate actin dynamics remain largely unknown.

Purpose of the Study:

To investigate how tensile force influences the dissociation kinetics of actin subunits.
To elucidate the molecular basis of force-dependent regulation of actin dynamics.

Main Methods:

Atomic force microscopy (AFM) force-clamp experiments were employed to measure dissociation kinetics.
Steered molecular dynamics (MD) simulations were utilized to explore force-induced structural changes.
Site-directed mutagenesis was performed on yeast actin to validate structural findings.

Main Results:

Tensile force alters G-actin/G-actin and G-actin/F-actin dissociation, exhibiting catch bonds at low forces and slip bonds above a threshold.
MD simulations revealed force-induced salt bridges, such as Lysine 113 (K113):Glutamic acid 195 (E195), contributing to catch-slip bond behavior.
Mutations K113S and E195S in yeast actin abolished the observed catch bond phenomenon.

Conclusions:

Actin filaments exhibit force-dependent catch-slip bond behavior, a novel mechanoregulatory mechanism.
A structural basis for actin catch-slip bonds involving specific inter-subunit interactions has been identified.
This mechanism may regulate cellular functions by controlling the depolymerization of force-bearing actin filaments.