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Related Concept Videos

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.
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...
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...
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.

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Related Experiment Video

Updated: May 10, 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

Structure and function of palladin's actin binding domain.

Moriah R Beck1, Richard D S Dixon, Silvia M Goicoechea

  • 1Department of Biochemistry and Biophysics, University of North Carolina School of Medicine, 120 Mason Farm Road, Chapel Hill, NC 27599, USA. moriah.beck@wichita.edu

Journal of Molecular Biology
|June 29, 2013
PubMed
Summary

Palladin

Keywords:
3D4′,6-diamidino-2-phenylindoleABPDAPIF-actinFLNaG-actinGFPHSQCPDBProtein Data BankRASRECVASPactin binding proteinactin-binding proteincrosslinkingelectrostaticsfilamentous actinfilamin Aglobular or monomeric actingreen fluorescent proteinheteronuclear single quantum correlationimmunoglubulin-like domainpalladinresolution-adapted structural recombinationthree-dimensionalvasodilator-stimulated phosphoprotein

More Related Videos

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
07:53

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

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: May 10, 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

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
07:53

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

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:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Palladin is a cell adhesion protein involved in actin organization.
  • The immunoglobulin 3 (Ig3) domain of palladin binds filamentous actin.
  • Understanding palladin's actin-binding mechanism is crucial for cell biology.

Purpose of the Study:

  • To determine the NMR structure of the palladin actin-binding domain.
  • To identify key residues and mechanisms involved in palladin-actin interactions.
  • To investigate the in vivo functional significance of palladin-actin binding.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy for structure determination.
  • Sedimentation equilibrium assays to assess protein self-association.
  • Site-directed mutagenesis to study palladin-actin interactions in vitro and in cells.

Main Results:

  • The NMR structure of the palladin Ig3 domain was elucidated.
  • Two basic patches on opposite faces of Ig3 were identified as critical for actin binding and cross-linking.
  • Palladin Ig3 does not self-associate, suggesting a mechanism for cross-linking two actin filaments.
  • Mutations disrupting actin binding altered cellular actin distribution and morphology.

Conclusions:

  • Palladin utilizes an electrostatic mechanism involving two basic patches on its Ig3 domain to cross-link actin filaments.
  • This interaction is essential for maintaining normal cellular actin organization and morphology in vivo.
  • The findings provide a structural and mechanistic basis for palladin's role in cell adhesion and actin dynamics.