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

Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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 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...
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...
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...

You might also read

Related Articles

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

Sort by
Same author

Measurement of the lifetime difference between Bs mass eigenstates.

Physical review letters·2005
Same author

Destruction of organic pollutants in reusable wastewater using advanced oxidation technology.

Chemosphere·2005
Same author

[A high performance liquid chromatographic method for the determination of teniposide in brain tissue using electro-chemical detection].

Se pu = Chinese journal of chromatography·2005
Same author

Correlating gene expression with chemical scaffolds of cytotoxic agents: ellipticines as substrates and inhibitors of MDR1.

The pharmacogenomics journal·2005
Same author

[Effects of cytokines on multidrug-resistance in K562/A02 cells].

Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi·2005
Same author

Analysis of the neuroligin 3 and 4 genes in autism and other neuropsychiatric patients.

Molecular psychiatry·2004

Related Experiment Video

Updated: Jul 28, 2026

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

Cdc42-induced actin filaments are protected from capping protein.

M Huang1, C Yang, D A Schafer

  • 1Biology Department University of Pennsylvania, Philadelphia, Pennsylvania 19104-6018, USA.

Current Biology : CB
|October 6, 1999
PubMed
Summary

Actin filament elongation is regulated by capping proteins. In neutrophil extracts, Cdc42-induced filaments are protected from capping, suggesting a novel regulatory mechanism for actin dynamics.

More Related Videos

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers
11:55

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers

Published on: July 12, 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

Related Experiment Videos

Last Updated: Jul 28, 2026

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

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers
11:55

Reconstitution of Membrane-Tethered Minimal Actin Cortices on Supported Lipid Bilayers

Published on: July 12, 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

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Actin filaments elongate primarily at their barbed ends.
  • Capping proteins bind barbed ends, terminating filament elongation.
  • Actin filament length is inversely related to capping protein concentration.

Purpose of the Study:

  • To investigate if capping protein regulates the length of actin filaments induced by Cdc42 in neutrophil extracts.
  • To determine if Cdc42-induced filaments are protected from capping.

Main Methods:

  • Manipulating capping protein concentration in neutrophil cell extracts.
  • Measuring actin filament lengths after nucleation with spectrin-actin seeds or Cdc42.
  • Assessing the effect of capping protein depletion and addition on filament lengths.

Main Results:

  • Depleting capping protein increased the length of spectrin-actin seeded filaments but not Cdc42-induced filaments.
  • Doubling capping protein concentration did not decrease the length of Cdc42-induced filaments.
  • These findings indicate Cdc42-induced filaments are resistant to capping.

Conclusions:

  • The barbed ends of Cdc42-induced actin filaments are protected from capping by capping protein.
  • This suggests a specific mechanism protects Cdc42-nucleated filaments from elongation termination.
  • Further research is needed to elucidate the protective mechanism.