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Related Concept Videos

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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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...
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Introduction to Actin01:26

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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...
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Actin Filament Depolymerization01:19

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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).
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Actin Polymerization and Cell Motility01:13

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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.
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Adaptability of Cytoskeletal Filaments01:12

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The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
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Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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Related Experiment Video

Updated: Apr 13, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Actin's functional "switch": Constraining C-terminal conformational flexibility disrupts functionally important

Karl E Steffensen1, John F Dawson1

  • 1Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada.

The Journal of Biological Chemistry
|April 12, 2026
PubMed
Summary

Actin

Keywords:
actinactomyosinallosteric communicationcomputational modelingmolecular dynamicsphenylenebismaleimideprotein structure

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Last Updated: Apr 13, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Actin's C-terminus is crucial for interactions with actin binding proteins (ABPs).
  • Understanding C-terminal conformational shifts has been limited by resolution constraints.
  • C-terminal shifts are influenced by nucleotide state and ABP binding.

Purpose of the Study:

  • To investigate the role of C-terminal shifts in actin's allosteric communication networks.
  • To understand how C-terminal modifications impact actin's functional state.
  • To explore how constraining C-terminal flexibility affects actin's conformation and communication.

Main Methods:

  • In silico modeling of actin filaments crosslinked by N,N'-para-phenylenebismaleimide (PBM).
  • Analysis of how PBM crosslinks affect distant structural elements and internal communication networks.
  • Examination of changes in nucleotide cleft architecture and dynamics.

Main Results:

  • Constraining C-terminal flexibility with PBM crosslinks reshapes allosteric communication networks.
  • Disruption of the F375-R116 interaction by PBM alters nucleotide cleft architecture.
  • PBM crosslinks impact nucleotide dynamics within the actin protomer.

Conclusions:

  • Actin's C-terminus acts as a nexus for structural changes, responding to stimuli.
  • C-terminal shifts propagate changes, enabling functional conformations and influencing ABP binding.
  • Allosteric communication networks are critical for regulating actin's dynamic functional states.