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関連する概念動画

Actin Polymerization01:42

Actin Polymerization

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 actin...
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.
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...
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...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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...

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関連する実験動画

Updated: Jul 4, 2026

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

電子的に活性化されたアクチンタンパク質のポリメリゼーションとアラインメント

Ian Y Wong1, Matthew J Footer, Nicholas A Melosh

  • 1Department of Materials Science & Engineering, Stanford University, Geballe Laboratory for Advanced Materials, 476 Lomita Mall, Stanford, California 94305, USA.

Journal of the American Chemical Society
|May 30, 2008
PubMed
まとめ

研究者は電子場を使用して,タンパク質のポリメリゼーションを動的に制御した. この方法は,アクチンフィラメントの形成を正確に制御し,バイオポリマー自己組み立ての応用を持つ新しいバイオミメティック材料を作成します.

科学分野:

  • バイオマテリアル科学 バイオマテリアル科学
  • バイオフィジックス 生物物理学
  • 分子生物学は分子生物学である.

背景:

  • 生物学的自己組み立ては,タンパク質の相互作用,イオン濃度,および改変の複雑な調整に依存しています.
  • 現在の生体模倣材料は,生物学的自己組み立てのダイナミックで多様な性質を複製するために苦労しています.

研究 の 目的:

  • 電子制御されたイオン混合とモノマー濃度を用いて,タンパク質ポリメリゼーションのダイナミックな調節を実証する.
  • 秩序あるマクロ分子構造の形成に対する前例のないコントロールを達成するために.

主な方法:

  • 低イオン強度バッファーを用いてアクチンポリメリゼーションを阻害する.
  • 低周波AC電圧でアクチンフィラメントの核化と成長を誘発し,局所単体濃度とMg2+) 混合を高めます.
  • 低周波 (100 Hz) と高周波 (1 MHz) の交流電圧の組み合わせを用いて,独立に制御されたポリメリゼーション率とフィラメントの方向性.

主要な成果:

  • イオン感受性タンパク質ポリメリゼーションの動的調節を達成した.
  • ポリメリゼーションの位置,範囲,速度,およびフィラメントの方向性に対する実証された電圧および周波数制御.
  • ハイドロゲル微粒子を含め, ~750 nm周期を持つアクチンフィラメント配列を並べた多様なマクロモレキュラーアーキテクチャを作成しました.

さらに関連する動画

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

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

Published on: July 11, 2025

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

関連する実験動画

Last Updated: Jul 4, 2026

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

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

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

Published on: July 11, 2025

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
06:54

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

Published on: June 3, 2021

結論:

  • 電子的に強化されたイオン混合とモノマー濃縮は,バイオポリマーの自己組み立てのダイナミック制御のための新しい方法を提供します.
  • このアプローチは,充電された種によって活性化される幅広い種類のタンパク質とバイオポリマーに潜在的に適用できます.
  • 複雑で秩序あるバイオミメティック構造の作成を可能にし,マクロ分子構造の正確な制御を可能にします.