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Updated: Jul 19, 2026

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
Published on: October 28, 2022
Arp2/3複合体とバキュロウイルスWASPのようなタンパク質によるダイナミックな核アクチン組成
Erin D Goley1, Taro Ohkawa, Joel Mancuso
1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
まとめ
バキュロウイルスは,Arp2/3複合体とウイルスタンパク質 (p78/83) を用いて核アクチンポリメリゼーションを誘導する. この核アクチンアセンブリは,新しいウイルス粒子の生成とウイルスの複製に不可欠です.
科学分野:
- ウイルス学 ウイルス学 ウイルス学
- 細胞生物学 細胞生物学
- 分子生物学は分子生物学である.
背景:
- 病原性細菌やウイルスは,しばしば宿主細胞のアクチンポリメリゼーションを,感染のために細胞質に操作します.
- 核アクチンダイナミクスは,細胞プロセスにおける役割としてますます認識されていますが,ウイルスによる操作はあまり理解されていません.
研究 の 目的:
- 宿主細胞核内のダイナミックなアクチンアセンブリを含む新しい病原性メカニズムを調査する.
- バキュロウイルス複製における核アクチンポリメリゼーションの役割を明らかにする.
主な方法:
- 利用したAutographa californica複数の核ポリヘドウイルス (AcMNPV) 感染モデル.
- 主体アクチン核化Arp2/3複合体の核への転移を調査した.
- ウイルスのウィスコット・オールドリッヒ症候群タンパク質 (WASP) のようなタンパク質p78/83が核アクチンアセンブリを活性化する機能を特徴付けました.
主要な成果:
- AcMNPVが核アクチンポリメリゼーションを誘導することを実証しました.
- ウイルスのタンパク質p78/83が,核内の宿主Arp2/3複合体を活性化することを示した.
- p78/83とArp2/3が媒介する核アクチンアセンブリが,ウイルスの子孫生成に不可欠であることを確認しました.
結論:
- 核アクチンポリメリゼーションは,バキュロウイルスで用いられる重要な病原性メカニズムである.
- ウイルスは,自己複製を促進するために宿主の核アクチンダイナミクスを操作することができます.
- 核アクチン再分割のこの戦略は,保存されたウイルス病原性メカニズムである可能性があります.
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...
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...
The high-order actin networks...
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 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...
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...
Introduction to Actin
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 different species.

