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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...

Actin Polymerization and Cell Motility

Actin Polymerization and Cell Motility

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.

Mechanism of Lamellipodia Formation

Mechanism of Lamellipodia Formation

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...

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...

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 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...

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Related Experiment Video

Updated: Jun 16, 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 polymerization overshoots induced by plus-end capping.

F J Brooks¹, A E Carlsson

¹Department of Physics, Washington University in Saint Louis, One Brookings Drive, St Louis, MO 63130, USA. fjbrooks@physics.wustl.edu

Physical Biology

|January 22, 2010

Summary

Transient polymerization overshoots in actin filaments can be explained by a decrease in plus-end polymerization due to capping. This finding offers new insights into actin dynamics and cellular mechanisms.

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Last Updated: Jun 16, 2026

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Area of Science:

Biochemistry
Cell Biology
Biophysics

Background:

Actin polymerization exhibits transient overshoots beyond steady-state levels.
Previous models focused on nucleotide hydrolysis states at filament plus-ends.

Purpose of the Study:

To investigate an alternative mechanism for actin polymerization overshoots.
To model the impact of plus-end capping on polymerization dynamics.

Main Methods:

Utilized rate equations to model polymerized actin concentration.
Analyzed the influence of initial filament concentration and capping rate.

Main Results:

Demonstrated decreasing plus-end polymerization contribution due to filament capping.
Developed an analytic formula linking overshoot magnitude to initial concentration and capping rate.
Identified high sensitivity of overshoot to these parameters.

Conclusions:

Plus-end capping of initial actin filaments explains observed polymerization overshoots.
The described dynamics are observable with current experimental techniques.
A cellular mechanism for amplifying these overshoots in vivo is proposed.