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

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...
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...
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...
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.
Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well characterized.

You might also read

Related Articles

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

Sort by
Same author

Inframalleolar Status According to the Global Limb Anatomic Staging System Is Associated With Wound Recurrence After Complete Wound Healing in Patients With Chronic Limb-Threatening Ischemia.

Journal of vascular surgery·2026
Same author

The Fate of Aortic Arch After Open Descending Thoracic and Thoracoabdominal Aortic Aneurysm Repair.

The Annals of thoracic surgery·2026
Same author

Effectiveness of a perforated spoon for reducing salt intake in a university cafeteria.

Frontiers in public health·2026
Same author

Isolated Endovascular Repair of the Ascending Aorta: Early Outcomes and Temporal Trends from a National Multicenter Registry.

Annals of vascular surgery·2026
Same author

Three-Year Outcomes of Supera Interwoven Nitinol Stents Versus Eluvia Drug-Eluting Stents in Severely Calcified Femoropopliteal Lesions.

Journal of vascular surgery·2026
Same author

Endoscopic vs. Operative Management of Acute Esophageal Perforation: A 21-Year Experience at a High-Volume Referral Center.

Seminars in thoracic and cardiovascular surgery·2026

Related Experiment Video

Updated: Jun 20, 2026

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
13:02

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Published on: December 28, 2019

NMR solution structures of actin depolymerizing factor homology domains.

Alexander K Goroncy1, Seizo Koshiba, Naoya Tochio

  • 1RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, Japan.

Protein Science : a Publication of the Protein Society
|September 22, 2009
PubMed
Summary

This study reveals novel structures of understudied actin-depolymerizing factor homology (ADF-H) domains, including the first mammalian drebrin-like and GMF beta structures. These findings offer new insights into actin binding mechanisms.

More Related Videos

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

Related Experiment Videos

Last Updated: Jun 20, 2026

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
13:02

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Published on: December 28, 2019

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

Area of Science:

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Actin dynamics are crucial for cellular processes and regulated by actin-depolymerizing factor homology (ADF-H) domains.
  • The ADF-H domain family comprises five classes, with ADF/cofilin being well-studied, while others like GMF, coactosin, twinfilin, and drebrin remain less characterized.
  • Limited structural data exists for most ADF-H domain classes, hindering a comprehensive understanding of their functions.

Purpose of the Study:

  • To determine the solution NMR structures of underrepresented ADF-H domains.
  • To provide the first structural insights into mammalian drebrin-like and GMF beta domains.
  • To elucidate structural differences related to actin binding across different ADF-H classes.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine protein structures.
  • Structural analysis focused on the ADF-H domains of human HIP-55-drebrin-like protein, mouse GMF beta and gamma, mouse coactosin-like domain, and mouse twinfilin 1 C-terminal domain.
  • Comparative structural analysis was performed to identify differences in actin-binding interfaces.

Main Results:

  • The study presents the first solution NMR structures of mammalian drebrin-like (human HIP-55) and GMF beta (mouse) domains.
  • Structures of mouse GMF gamma, mouse coactosin-like domain, and mouse twinfilin 1 C-terminal ADF-H domain were also determined.
  • Significant structural variations, particularly in actin-binding regions and the presence of additional beta-strands in GMF beta/gamma, were identified compared to other ADF-H domains.

Conclusions:

  • The determined structures provide valuable insights into the distinct mechanisms of globular actin (G-actin) and filamentous actin (F-actin) binding among ADF-H domain classes.
  • The identification of specific binding residues on the central helix and unique structural features in GMF beta/gamma advance the understanding of actin regulation.
  • This work lays the foundation for further functional studies on these less-explored ADF-H domain families.