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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.2K
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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Introduction to Actin01:26

Introduction to Actin

5.3K
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...
5.3K
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

3.2K
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...
3.2K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

5.4K
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....
5.4K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.5K
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...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.0K
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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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Aip1p Dynamics Are Altered by the R256H Mutation in Actin

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アクチン結合タンパク質の機能に対する,急性サイトカリシンBによる差異的干渉

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
まとめ
この要約は機械生成です。

サイトカラーシンB (CB) とD (CD) は,先程考えられていたようにポリメリゼーションを阻害せず,刺さった末端結合タンパク質の蓄積を強化することによって,アクチンダイナミクスを変化させます. 細胞の構造に及ぼす影響について 新たな洞察を得ました

キーワード:
Arp2/3 コンプレックスエナ/VASPアクティンの売上高キャピングタンパク質サイトカルシンin vitro 再構成ラメリポディアムローカル アプリケーション作用形態突出する

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Simplified, High-throughput Analysis of Single-cell Contractility using Micropatterned Elastomers
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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
07:53

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

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関連する実験動画

Last Updated: Sep 8, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
08:57

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

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Simplified, High-throughput Analysis of Single-cell Contractility using Micropatterned Elastomers
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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
07:53

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin

Published on: March 28, 2008

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科学分野:

  • 細胞生物学
  • 生物化学
  • 分子生物学

背景:

  • アクチンフィラメントのダイナミクスは細胞プロセスにとって不可欠です.
  • サイトカラーシンB (CB) とD (CD) は,アクチンダイナミクスを研究するために一般的に使用されます.
  • アクチンの刺さった端の正確な分子機構は完全に理解されていません.

研究 の 目的:

  • 動的細胞構造におけるアクチンフィラメントの端結合タンパク質に対するCBの分子効果を調査する.
  • CBがラメリポディアのアクチンダイナミクスに影響を与える正確なメカニズムを解明する.

主な方法:

  • 光アクチン結合タンパク質の活体細胞イメージング
  • 移動する細胞におけるラメリポディアの急性治療
  • アクチンネットワークに対するCB効果の in vitro 再構成

主要な成果:

  • CBはラメリポディアムの突起を止めますが,エナ/VASPやキャピングタンパク質 (CP) のような刺さった末端結合タンパク質の蓄積を高めます.
  • CB誘発のVASP蓄積はCPに依存し,アクチンとVASPの回転を減少させます.
  • 実験室での研究では,CBがVASPの停留時間を長引くことが示されています.

結論:

  • サイトカラシンは,ポリメリゼーションを阻害することとは異なる,刺さった末端結合因子に対する新しい活性を示します.
  • これらの発見は,CBとCDが細胞内のダイナミックなアクチン構造にどのように影響するかを再評価することを必要としています.
  • この結果は,細胞生物学におけるシトカライシンを用いた実験の解釈に不可欠な新しい情報を提供します.