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

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.0K
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...
3.0K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.0K
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...
3.0K
Actin Polymerization01:42

Actin Polymerization

6.8K
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...
6.8K
Introduction to Actin01:26

Introduction to Actin

5.3K
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...
5.3K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.2K
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...
3.2K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.4K
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...
2.4K

You might also read

Related Articles

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

Sort by
Same author

Red blood cell distribution width to albumin ratio and systemic immune-inflammatory index as predictors of mortality in severe pneumonia: A retrospective cohort analysis.

PloS one·2026
Same author

Wedelactone-loaded exosomes for sepsis-induced liver injury: a novel therapeutic strategy.

Drug delivery·2026
Same author

Targeting the crosstalk between Alzheimer's disease and gastrointestinal cancers.

Molecular medicine (Cambridge, Mass.)·2026
Same author

The anti-respiratory syncytial virus activity of biochemicals from Pyrola incarnata.

Antiviral research·2026
Same author

A Field-Deployable Microfluidic CNT-FET Platform for Direct Monitoring of Multiplexed Respiratory Viruses in Environmental Waters.

ACS sensors·2026
Same author

tRF and gastric cancer: molecular mechanism exploration and novel strategies for precision diagnosis and therapy.

Journal of translational medicine·2026

Related Experiment Video

Updated: Aug 24, 2025

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

2.7K

Bending forces and nucleotide state jointly regulate F-actin structure.

Matthew J Reynolds1, Carla Hachicho1, Ayala G Carl1,2

  • 1Laboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA.

Nature
|October 26, 2022
PubMed
Summary

Actin filament (F-actin) nucleotide state influences its structure when bent. Phosphate presence rigidifies actin, altering mechanical regulation and potentially guiding actin-binding proteins.

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

1.8K
Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones
09:14

Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones

Published on: March 17, 2011

14.9K

Related Experiment Videos

Last Updated: Aug 24, 2025

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

2.7K
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

1.8K
Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones
09:14

Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones

Published on: March 17, 2011

14.9K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Actin polymerization is key to cellular force generation.
  • Actin filament (F-actin) dynamics are regulated by force and nucleotide state, but mechanisms remain unclear.

Purpose of the Study:

  • To investigate how actin nucleotide state modulates F-actin structural transitions under bending forces.
  • To elucidate the role of actin nucleotide state in mechanical regulation of F-actin.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine structures of ADP-F-actin and ADP-Pi-F-actin.
  • Machine-learning pipeline for reconstructing bent F-actin structures with high resolution.
  • Analysis of intersubunit interfaces and conformational changes in bent filaments.

Main Results:

  • ADP-F-actin and ADP-Pi-F-actin lattices are nearly identical at low resolution, with minimal backbone differences.
  • Bent F-actin structures reveal distinct rearrangements at intersubunit interfaces, including altered helical twist and protomer deformations.
  • Phosphate appears to rigidify actin subunits, influencing the bending structural landscape.

Conclusions:

  • Actin nucleotide state significantly modulates F-actin's response to bending forces.
  • Conformational transitions in bent F-actin are nucleotide-state dependent and large enough to be detected by actin-binding proteins.
  • Actin nucleotide state acts as a co-regulator of F-actin mechanical properties.