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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.
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...
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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.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
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Actin Treadmilling01:18

Actin Treadmilling

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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
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Introduction to Actin01:26

Introduction to Actin

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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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Olefin Metathesis Polymerization: Ring-Opening Metathesis Polymerization (ROMP)01:16

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Ring-opening metathesis polymerization or ROMP involves strained cycloalkenes as starting materials. The mechanism of ROMP proceeds by reacting cycloalkene with Grubbs catalyst to give metallacyclobutane intermediate which undergoes a ring-opening reaction to form new carbene. The new carbene reacts with another molecule of cycloalkene. Repetition of these steps leads to the formation of an unsaturated open-chain polymer product. All these steps are reversible, however, relieving the ring...
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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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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).
In F-actin, the ADF/cofilin proteins...
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In Vitro Polymerization of F-actin on Early Endosomes
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Actin polymerization is activated by terahertz irradiation.

Shota Yamazaki1,2, Masahiko Harata3, Toshitaka Idehara4

  • 1Laboratory of Molecular Biology, Graduate School of Agricultural Science, Tohoku University, Aramaki Aza Aoba 468-1, Aoba-ku, Sendai, 980-0845, Japan. shota.yamazaki.fc@riken.jp.

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Terahertz (THz) wave irradiation activates actin polymerization, a key process in cell functions. This novel method significantly increased actin filament formation, offering new ways to manipulate biomolecules and cells.

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Area of Science:

  • Biophysics
  • Cell Biology
  • Biomolecular Engineering

Background:

  • Actin polymerization into filaments is crucial for cellular processes like motility, growth, differentiation, and gene expression.
  • Existing methods to manipulate actin polymerization include actin-binding chemicals, essential for biological research and therapeutic applications.

Purpose of the Study:

  • To investigate terahertz (THz) waves as a novel method for modulating actin polymerization.
  • To explore the potential of THz irradiation in controlling biological functions at the molecular level.

Main Methods:

  • Actin polymerization reactions were conducted under irradiation with 0.46 THz waves generated by a Gyrotron.
  • Actin polymerization was monitored using pyrene actin fluorophores to assess activation.
  • The number of actin filaments was quantified using fluorescence microscopy with the SiR-actin probe.

Main Results:

  • Terahertz wave irradiation significantly activated actin polymerization.
  • A 3.5-fold increase in actin filaments was observed after 20 minutes of THz irradiation.
  • THz irradiation enhanced actin polymerization even in a steady-state solution, indicating activation of the elongation process.

Conclusions:

  • Terahertz waves represent a novel and effective tool for modulating actin polymerization.
  • This finding suggests potential applications of THz waves in manipulating biomolecules and cells for research and therapeutic purposes.