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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).
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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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Generation of Straight or Branched Actin Filaments01:14

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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.
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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 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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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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ADPact: A versatile sensor for ADP-F-actin.

Qianqian Ma1, Xiao Han1, Kexin Zhu1

  • 1School of Biological Sciences, Nanyang Technological University, Singapore 637551, Singapore.

Proceedings of the National Academy of Sciences of the United States of America
|July 16, 2025
PubMed
Summary

Scientists developed ADPact, a peptide that visualizes ADP-bound actin filaments (F-actin). This tool accurately monitors cytoskeletal dynamics without disruption, offering new insights into cellular processes.

Keywords:
ADP-F-actinADPactactin cytoskeleton

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Area of Science:

  • Cell Biology
  • Biochemistry

Background:

  • The actin cytoskeleton's dynamic organization is vital for cellular functions.
  • Regulation relies on the nucleotide state of actin filaments (F-actin).
  • Specific visualization of ADP-bound F-actin is currently limited.

Purpose of the Study:

  • To develop a novel tool for specifically visualizing ADP-bound F-actin.
  • To enable accurate monitoring of actin dynamics in vitro and in cells.
  • To investigate actin regulation under varying energy conditions.

Main Methods:

  • Introduction of ADPact, a 20-amino-acid peptide with selective binding to ADP-F-actin.
  • Application of ADPact and its fluorescent variant, ADPact-GFP, for visualization.
  • Testing in vitro and in eukaryotic cells, including under energy stress.

Main Results:

  • ADPact selectively binds to ADP-F-actin.
  • ADPact and ADPact-GFP allow precise visualization of ADP-F-actin structures.
  • The tool does not disrupt actin dynamics, ensuring reliable monitoring.

Conclusions:

  • ADPact is a powerful new tool for studying actin dynamics.
  • It provides insights into cytoskeleton regulation in physiological and pathological states.
  • Useful for visualizing ADP-F-actin, especially during energy stress.