Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
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...
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 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.
Mechanism of Filopodia Formation01:39

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.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Association of bidi smoking and tobacco-use patterns with cancer risk in India: a multicentre unmatched case-control study (2024-2025).

The Lancet regional health. Southeast Asia·2026
Same author

Incidental Radiation Exposure to the Internal Mammary Lymph Nodes in Breast Cancer Patients Undergoing Intensity-Modulated Radiation Therapy: A Retrospective Analysis.

The Gulf journal of oncology·2026
Same author

To Intervene or Not to Intervene: Rethinking Non-culprit Vessels in Acute Coronary Syndrome.

Journal of cardiothoracic and vascular anesthesia·2026
Same author

Leiomodin 2 functions as a processive pointed-end elongator of actin filaments.

bioRxiv : the preprint server for biology·2026
Same author

Structural rewiring of the mannose-binding pocket reveals adaptive FimH mutations that enhance uroplakin-associated glycan recognition and uropathogenic adhesion.

International journal of biological macromolecules·2026
Same author

Challenges in the Early Diagnosis, Screening and Management of Heart Failure in Patients with Chronic Obstructive Pulmonary Disease.

Journal of clinical medicine·2026
Same journal

Hunting ecology predicts eye arrangements in the modular visual system of spiders.

Current biology : CB·2026
Same journal

Sub-second fluctuations between top-down and bottom-up modes distinguish diverse human brain states.

Current biology : CB·2026
Same journal

Queen bees offload pesticide burden to eggs when social buffering is overwhelmed.

Current biology : CB·2026
Same journal

Pitch selectivity in ferret auditory cortex.

Current biology : CB·2026
Same journal

A cell size-dependent competition between geometry and polarity governs nuclear and spindle positioning in early embryos.

Current biology : CB·2026
Same journal

Trophic cascades drive sustainability in the agricultural heritage rice-fish coculture system.

Current biology : CB·2026
See all related articles

Related Experiment Video

Updated: Jun 10, 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

Actin dynamics: Filament end remodeling drives rapid depolymerization.

Shashank Shekhar1

  • 1Departments of Physics, Cell Biology and Biochemistry, Emory University, Atlanta, GA 30322, USA.

Current Biology : CB
|June 8, 2026
PubMed
Summary
This summary is machine-generated.

Actin filament turnover is rapid but poorly understood. New cryo-EM structures show cofilin and cyclase-associated protein create monomer-like states at filament ends, promoting dissociation and subunit loss.

More Related Videos

Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

Published on: July 11, 2025

Related Experiment Videos

Last Updated: Jun 10, 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

Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

Published on: July 11, 2025

Area of Science:

  • Cellular biology
  • Biochemistry
  • Structural biology

Background:

  • Actin filaments are crucial for cell structure and motility.
  • Rapid actin filament turnover is essential for dynamic cellular processes.
  • The structural mechanisms driving rapid actin turnover remain largely unknown.

Purpose of the Study:

  • To elucidate the structural basis of rapid actin filament turnover.
  • To investigate the roles of cofilin and cyclase-associated protein in actin dynamics.

Main Methods:

  • High-resolution cryo-electron microscopy (cryo-EM).
  • Structural analysis of actin filament ends.

Main Results:

  • Cofilin and cyclase-associated protein remodel actin filament ends.
  • These proteins convert filament ends into monomer-like states.
  • This remodeling promotes capping protein dissociation, accelerates subunit loss, and suppresses reassembly.

Conclusions:

  • Cofilin and cyclase-associated protein are key regulators of actin filament depolymerization.
  • Structural remodeling of filament ends by these proteins explains rapid actin turnover.
  • Understanding these mechanisms provides insight into cellular actin dynamics.