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Quantitative Analysis of Cell Edge Dynamics during Cell Spreading
Published on: May 22, 2021
N-WASPの交換率は,ARP2/3複合体依存のアクチンベースの運動性の範囲を制限する
Ina Weisswange1, Timothy P Newsome, Sibylle Schleich
1Cell Motility Laboratory, Cancer Research UK, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.
Nature
|March 6, 2009
まとめ
病原体のアクチンベースの運動性は,局所的なシグナル伝達に依存しています. ニューロンのウィスコット・オールドリッチ症候群タンパク質 (N-WASP) の動態を研究し,その交換率がアクチンポリメリゼーションを調節することによってウイルスの動きを制御することを発見しました.
科学分野:
- 細胞生物学 細胞生物学
- 分子生物学は分子生物学である.
- ウイルス学 ウイルス学 ウイルス学
背景:
- 細胞の運動性を理解するには,アクチンポリメリゼーションのシグナルダイナミクスに関する知識が必要です.
- 病原体のアクチンベースの運動経路は,局所的なシグナルダイナミクスを研究するためのモデルを提供します.
研究 の 目的:
- ニューロンのウィスコット・オルドリッヒ症候群タンパク質 (N-WASP),WASP相互作用タンパク質 (WIP),GRB2,およびNCKが,ワクチンウイルスのアクチンベースの運動性におけるダイナミクスを分析する.
- タンパク質のダイナミクスがアクチンポリメリゼーションの速度とウイルスの移動にどのように影響するか調査する.
主な方法:
- タンパク質のダイナミクスを測定するために,光漂白後の光回復 (FRAP) を利用しました.
- GRB2とアクチンフィラメントとのN-WASP相互作用の役割を調査した.
主要な成果:
- N-WASP,WIP,GRB2,NCKは,運動期間に急速に交換する.
- N-WASPのターンオーバーは,ARP2/3複合体によるアクチンポリメリゼーションを刺激する能力と関連しています.
- N-WASPの相互作用を妨害することで,ウイルスの移動が加速された.
結論:
- N-WASPの為替レートはARP2/3-複合体依存運動性を調節する.
- N-WASPは,アクチンポリメリゼーションとフィラメントキャピングを調節することによって,運動性を制御します.
関連する概念動画
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...
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...
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...
In F-actin, the ADF/cofilin proteins...
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.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
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...
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...
Mechanism of Lamellipodia Formation
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...
Actin Treadmilling
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...

