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Related Concept Videos

Actin Polymerization01:42

Actin Polymerization

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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.
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Mechanism of Filopodia Formation01:39

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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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Formation of Intermediate Filaments00:57

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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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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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Mechanism of Lamellipodia Formation01:31

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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Disassembly of Intermediate Filaments01:35

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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Updated: May 2, 2026

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
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Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

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Relationship Between Filament-Polymerizing Muscle Myosin and Droplets Generated by Liquid-Liquid Phase Separation.

Tatsuyuki Waizumi1, Mahito Kikumoto1, Tomoharu Matsumoto1

  • 1Department of Biological Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi, Japan.

Chembiochem : a European Journal of Chemical Biology
|May 1, 2026
PubMed
Summary
This summary is machine-generated.

Liquid-liquid phase separation (LLPS) influences myosin behavior in polymer solutions, causing it to form filament meshworks within droplets. Myosin, in turn, deforms these droplets, altering their morphology and even inducing protrusions.

Keywords:
droplet deformationfilament polymerizationliquid–liquid phase separationmuscle myosinprotrusion formation of droplet

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Area of Science:

  • Biophysics
  • Cell Biology
  • Polymer Science

Background:

  • Biological systems utilize macromolecules like nucleic acids and proteins within internal fluids.
  • Liquid-liquid phase separation (LLPS) explains complex macromolecular phenomena within cells.
  • LLPS principles extend from cellular scales to larger biological organizations.

Purpose of the Study:

  • Investigate the interplay between myosin motor protein behavior and LLPS.
  • Examine how myosin interacts with and influences LLPS in a binary polymer solution.
  • Understand the impact of myosin's presence on droplet formation and morphology.

Main Methods:

  • Utilized a binary polymer solution composed of polyethylene glycol and dextran.
  • Introduced myosin, a muscle-derived molecular motor, into the polymer solution.
  • Varied salt concentrations to observe effects on myosin polymerization and LLPS.

Main Results:

  • Myosin localized within dextran-rich phase droplets.
  • Myosin polymerized into filaments and formed mesh-like assemblies within droplets, irrespective of salt-induced polymerization conditions.
  • The presence of myosin induced deformation of the LLPS droplets, leading to non-spherical shapes.
  • At specific salt strengths, myosin-containing droplets exhibited sharp protrusions.

Conclusions:

  • LLPS significantly alters myosin's behavior and assembly dynamics within droplets.
  • Myosin's presence and polymerization impact the morphology and stability of LLPS droplets.
  • This study reveals a reciprocal relationship between molecular motors and phase-separated biomolecular condensates.