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Related Concept Videos

Actin Treadmilling01:18

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...
Actin Polymerization01:42

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 Filament Depolymerization01:19

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 Filaments01:14

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...
Introduction to Actin01:26

Introduction to Actin

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 different species.
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...

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Related Experiment Video

Updated: Jun 24, 2026

Monitoring Actin Disassembly with Time-lapse Microscopy
06:12

Monitoring Actin Disassembly with Time-lapse Microscopy

Published on: November 8, 2006

Double JMY: making actin fast.

David W Roadcap, James E Bear

    Nature Cell Biology
    |April 2, 2009
    PubMed
    Summary
    This summary is machine-generated.

    A newly identified protein, JMY, possesses dual nucleation-promoting activities crucial for actin network assembly. This protein shuttles between cellular compartments, significantly impacting cell migration and actin dynamics in motile cells.

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    Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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    Aip1p Dynamics Are Altered by the R256H Mutation in Actin
    08:57

    Aip1p Dynamics Are Altered by the R256H Mutation in Actin

    Published on: July 30, 2014

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    Last Updated: Jun 24, 2026

    Monitoring Actin Disassembly with Time-lapse Microscopy
    06:12

    Monitoring Actin Disassembly with Time-lapse Microscopy

    Published on: November 8, 2006

    Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
    08:02

    Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

    Published on: May 5, 2022

    Aip1p Dynamics Are Altered by the R256H Mutation in Actin
    08:57

    Aip1p Dynamics Are Altered by the R256H Mutation in Actin

    Published on: July 30, 2014

    Area of Science:

    • Cell Biology
    • Molecular Biology
    • Biochemistry

    Background:

    • Actin network assembly is essential for cellular functions.
    • Nucleation-promoting factors (NPFs) regulate actin polymerization.
    • The role of specific NPFs in cell motility remains an area of active research.

    Discussion:

    • JMY protein exhibits two distinct nucleation-promoting activities.
    • JMY dynamically shuttles between the nucleus and cytoplasm.
    • This nucleocytoplasmic shuttling influences JMY's function in actin regulation.

    Key Insights:

    • JMY acts as a critical regulator of actin dynamics.
    • The dual nucleation-promoting activities of JMY are novel.
    • JMY's localization dynamics are linked to its functional role.

    Outlook:

    • Further investigation into JMY's precise molecular mechanisms.
    • Exploring JMY's role in various physiological and pathological processes.
    • Potential therapeutic targeting of JMY for controlling cell migration.