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Related Concept Videos

Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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 networks...
Actin Polymerization and Cell Motility01:13

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.
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...
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...
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

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...
Cytoskeletal Coordination in Cell Migration01:32

Cytoskeletal Coordination in Cell Migration

A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker proteins that...

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Related Experiment Video

Updated: Jun 8, 2026

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

Direct dynamin-actin interactions regulate the actin cytoskeleton.

Changkyu Gu1, Suma Yaddanapudi, Astrid Weins

  • 1Nephrology Division, Department of Medicine, Harvard Medical School and Massachusetts General Hospital, Charlestown, MA 02129, USA.

The EMBO Journal
|October 12, 2010
PubMed
Summary
This summary is machine-generated.

Dynamin directly binds actin filaments, promoting their bundling and polymerization. This interaction is crucial for regulating cell shape and membrane dynamics, revealing a novel mechanism for actin cytoskeleton control.

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Last Updated: Jun 8, 2026

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

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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy
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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Cytoskeleton Dynamics

Background:

  • The large GTPase dynamin is known to be involved in endocytosis.
  • Dynamin also regulates the actin cytoskeleton via an unknown GTPase-dependent mechanism.

Purpose of the Study:

  • To elucidate the mechanism by which dynamin regulates the actin cytoskeleton.
  • To identify the direct interaction between dynamin and actin filaments.

Main Methods:

  • Identification of a conserved actin-binding site in dynamin.
  • Analysis of point mutations in the dynamin actin-binding domain.
  • In vitro assays to study dynamin assembly and gelsolin displacement.

Main Results:

  • Dynamin directly binds and bundles actin filaments through a conserved site.
  • Mutations in this site lead to defects in membrane ruffling and actin stress fibers.
  • Assembled dynamin, stimulated by short actin filaments, displaces gelsolin, promoting actin elongation.

Conclusions:

  • Dynamin directly interacts with actin filaments, bundling them and promoting polymerization.
  • This interaction provides a novel mechanism for dynamin-mediated regulation of the actin cytoskeleton.
  • Findings shed light on dynamin's role in cellular processes beyond endocytosis.