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Related Concept Videos

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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Introduction to Actin01:26

Introduction to Actin

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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 Polymerization01:42

Actin Polymerization

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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.
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...
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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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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
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The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Related Experiment Video

Updated: Feb 10, 2026

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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The actin-related proteins

S Frankel1, M S Mooseker

  • 1Department of Biology, Yale University, New Haven, CT 06520-8103, USA. Stewart_frankel@qm.yale.edu

Current Opinion in Cell Biology
|February 1, 1996
PubMed
Summary
This summary is machine-generated.

Actin-related proteins (Arps) are a diverse protein family expanding rapidly. Recent studies link Arps to crucial cellular functions involving actin filaments, microtubules, and chromatin structure.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • A rapidly expanding family of actin-related proteins (Arps) exhibits structural and functional diversity distinct from actin.
  • Arps belong to a larger superfamily including actins, hsp/hsc70s, sugar kinases, and bacterial cell cycle proteins.
  • The superfamily's existence is inferred from tertiary structural data, while Arps are identified and classified using primary structural data.

Purpose of the Study:

  • To explore the expanding family of actin-related proteins (Arps).
  • To understand the functional roles of different Arps within the cell.
  • To classify Arps based on primary structural data and explore their superfamily connections.

Main Methods:

  • Sequence homology analysis for identification and classification of Arps.
  • Tertiary structural data analysis to infer superfamily relationships.
  • Genetic and biochemical analyses to determine Arp functions.

Main Results:

  • Arps show significant sequence homology to actin but possess distinct structural and functional properties.
  • Arps are part of a larger superfamily, suggesting conserved evolutionary origins.
  • Specific Arps have been functionally linked to actin filaments (Arp2, Arp3), microtubules (Arp1), and chromatin structure (Arp4, Arp6).

Conclusions:

  • The actin-related protein family is diverse and expanding, with members playing varied cellular roles.
  • Functional characterization of Arps is progressing, revealing connections to cytoskeletal dynamics and nuclear processes.
  • Arps represent a significant branch of a conserved protein superfamily, highlighting fundamental biological mechanisms.