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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.
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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.
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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.
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Related Experiment Video

Updated: May 28, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Actin interacting protein1 and actin depolymerizing factor drive rapid actin dynamics in Physcomitrella patens.

Robert C Augustine¹, Kelli A Pattavina, Erkan Tüzel

¹Biology Department, University of Massachusetts, Amherst, Massachusetts 01003, USA.

|October 18, 2011

Summary

Actin interacting protein1 (AIP1) and actin depolymerizing factor (ADF) are crucial for plant cell growth. Our study reveals AIP1 promotes, while ADF is essential for, actin dynamics necessary for tip growth in moss.

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Last Updated: May 28, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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Published on: July 30, 2014

Real-time Imaging of Plant Cell Surface Dynamics with Variable-angle Epifluorescence Microscopy

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Published on: December 12, 2015

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Area of Science:

Plant cell biology
Molecular plant science
Cytoskeletal dynamics

Background:

Actin network remodeling is vital for eukaryotic cellular processes.
Several actin-binding proteins are implicated in plant cortical actin filament (F-actin) remodeling.
The in planta function of these proteins in F-actin dynamics remains largely uncharacterized.

Purpose of the Study:

To investigate the in vivo function of actin interacting protein1 (AIP1) and actin depolymerizing factor (ADF) in plant actin dynamics.
To determine the genetic relationship between AIP1 and ADF in promoting tip growth.
To elucidate the roles of AIP1 and ADF in regulating F-actin organization and dynamics.

Main Methods:

Reverse genetics in Physcomitrella patens.
Complementation analyses.
Cell biological approaches including F-actin staining and live-cell imaging.

Main Results:

AIP1 is a single-copy gene in P. patens; AIP1 knockout plants exhibit reduced tip-growing cell expansion.
AIP1 and ADF function in a common genetic pathway to promote tip growth, with ADF partially compensating for AIP1 loss.
AIP1 knockout lines show increased F-actin bundles, reduced dynamic ends, and decreased severing frequency, indicating impaired actin remodeling.
AIP1 promotes F-actin dynamics, while ADF is essential for these dynamics.

Conclusions:

AIP1 plays a significant role in promoting cortical F-actin dynamics essential for tip growth in plants.
ADF is indispensable for these dynamics, highlighting a synergistic relationship between AIP1 and ADF.
Understanding these actin-binding proteins provides insights into cytoskeletal regulation in plant development.