封闭蛋白通过促进Arp2/3复合体的丝核化来增加基于actin的运动率
1Department of Cellular and Molecular Pharmacology, School of Medicine, University of California, San Francisco, San Francisco, CA 94143, USA.
Cell
|May 31, 2008
概括
覆盖蛋白 (CP) 通过促进Arp2/3复杂的活性丝核化而不是延长,增强了阿米体的运动性. 这种协同作用驱动着运动率,而活性质组装率保持不变.
科学领域:
- 细胞生物学 细胞生物学
- 生物化学 生物化学
- 生物物理学的生物物理.
背景情况:
- 封闭蛋白 (CP) 调节了行动蛋白丝的动态.
- 由Arp2/3复合体核化的动素网络对于阿米的运动性至关重要.
研究的目的:
- 为了研究封闭蛋白和Arp2/3复合体在驱动基于actin的运动性之间的协同关系.
- 阐明限制蛋白质影响运动率的机制.
主要方法:
- 使用纯化蛋白质进行体外基于actin的运动系统的复制.
- 在不同蛋白质度下,对actin线丝动态和运动率的定量分析.
主要成果:
- 覆盖蛋白通过增加Arp2/3介导的氨酸丝核的频率来增强运动性.
- 通过封闭蛋白质,行为丝延长的速度不会直接增加.
- 活性蛋白组合的净速率独立于限制蛋白质和Arp2/3复合物的度.
结论:
- 封闭蛋白和Arp2/3复合体之间的协同作用对于调节阿米体运动性至关重要.
- 由封闭蛋白和Arp2/3影响的动丁网络架构决定了运动率.
- 这项研究揭示了一种新的机制,它结合了actin核和限制蛋白质功能.
相关概念视频
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 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...
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 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...
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...
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...


