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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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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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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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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.
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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.
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Differential interference with actin-binding protein function by acute cytochalasin B.

Christopher Lambert1, Marius Karger2, Xinqi Jiang2

  • 1Molecular Cell Biology Group, Helmholtz Centre for Infection Research (HZI), Inhoffenstraße 7, 38124 Braunschweig, Germany; Division of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig, Spielmannstraße 7, 38106 Braunschweig, Germany; Department of Microbial Drugs, Helmholtz Centre for Infection Research (HZI), German Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany.

Current Biology : CB
|September 6, 2025
PubMed
Summary
This summary is machine-generated.

Cytochalasin B (CB) and D (CD) alter actin dynamics by enhancing barbed end-binding protein accumulation, not blocking polymerization as previously thought. This reveals new insights into their effects on cell structures.

Keywords:
Arp2/3 complexEna/VASPactin turnovercapping proteincytochalasinin vitro-reconstitutionlamellipodiumlocal applicationmode of actionprotrusion

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Actin filament dynamics are essential for cellular processes.
  • Cytochalasin B (CB) and D (CD) are commonly used to study actin dynamics.
  • Their precise molecular mechanisms on actin barbed ends are not fully understood.

Purpose of the Study:

  • To investigate the molecular effects of CB on actin filament barbed end-binding proteins in dynamic cellular structures.
  • To elucidate the precise mechanisms by which CB influences actin dynamics in lamellipodia.

Main Methods:

  • Live cell imaging of fluorescent actin-binding protein dynamics.
  • Acute treatment of lamellipodia in migrating cells with CB.
  • In vitro reconstitution of CB effects on actin networks.

Main Results:

  • CB halts lamellipodium protrusion but enhances accumulation of barbed end-binding proteins like Ena/VASP and capping protein (CP).
  • CB-induced VASP accumulation depends on CP and reduces actin and VASP turnover.
  • In vitro studies show CB increases VASP dwell time on filament barbed ends.

Conclusions:

  • Cytochalasins exhibit a novel activity on barbed end-binding factors, distinct from blocking polymerization.
  • These findings necessitate a re-evaluation of how CB and CD affect dynamic actin structures in cells.
  • The results provide critical new information for interpreting experiments using cytochalasins in cell biology.