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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.
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.
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...
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...
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...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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Updated: Jul 8, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

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Published on: July 30, 2014

Evolutionarily conserved short linear motifs drive actin filament binding.

Themistoklis Paraschiakos1, Biao Yuan2,3,4,5, Michael Hecht-Bucher1

  • 1Department of Biochemistry and Signal Transduction, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.

Nature Cell Biology
|July 6, 2026
PubMed
Summary

Researchers identified a new actin-binding motif (SFM) in 103 human proteins. This motif regulates actin filament structure and stiffness, connecting cellular dynamics to diverse functions.

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Last Updated: Jul 8, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Published on: July 30, 2014

Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

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

Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Actin cytoskeleton regulation by actin-binding proteins is crucial for cellular homeostasis.
  • The specific binding mode of actin-binding proteins dictates their cellular activity.

Purpose of the Study:

  • To identify and characterize a novel actin filament-binding motif.
  • To explore the prevalence and evolutionary origins of this motif.
  • To understand how this motif influences actin filament properties and cellular functions.

Main Methods:

  • Cryo-electron microscopy was used to determine the structure of the ITPKA-actin filament complex.
  • The computational pipeline SLiMFold was employed to discover proteins containing the motif.
  • Phylogenetic analysis was conducted to assess evolutionary conservation.
  • Actin filament-binding affinities were measured.
  • Cryo-electron microscopy structures of SFM-actin filament complexes were determined.

Main Results:

  • A 'short linear actin filament-binding motif' (SFM) was identified.
  • 103 human proteins containing SFMs were discovered, involved in diverse cellular roles.
  • SFMs are conserved across eukaryotes and arose de novo.
  • SFMs exhibit actin filament-binding affinities in the range of 2-12 µM.
  • SFM binding was shown to decrease actin-filament stiffness.

Conclusions:

  • SFMs act as anchoring modules, linking actin dynamics to various cellular functions.
  • The identified motif regulates actin filament conformation and mechanical properties.
  • This discovery provides a framework for understanding the roles of numerous actin-associated proteins.