雅丁丝尖端封闭的机制是由tropomodulin进行的
Jampani Nageswara Rao1, Yadaiah Madasu1, Roberto Dominguez2
1Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
概括
特罗波莫杜林 (Tmod) 覆盖了缓慢生长的状丝的尖端. 结构和生化研究表明,Tmod 结合了三种actin子单元和两种tropomyosins,从而实现了可控的尖端动态.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 细胞生物学 细胞生物学
背景情况:
- 动氨酸纤维对细胞骨动力学至关重要.
- 特罗波莫杜林 (Tmod) 是唯一已知的蛋白质,可以封闭丝丝的尖端.
- 由于缺乏结构数据,Tmod的上限机制仍然不太清楚.
研究的目的:
- 阐明特罗波莫杜林 (Tmod) 尖端封闭机制的结构基础.
- 了解Tmod如何调节尖端的actin导线动态.
主要方法:
- 进行X射线晶体学以确定actin-Tmod复合物的结构.
- 对Tmod域和结构灵感突变的生物化学分析.
- 研究Tmod与actin和tropomyosin的相互作用.
主要成果:
- 晶体结构揭示了Tmod与尖端的三个actin子单元的相互作用.
- 此外,Tmod还与光线的两侧的托罗普米奥辛分子接触.
- 高亲和度结合是通过多个低亲和度相互作用实现的.
结论:
- 这种Tmod限制机制涉及与actin和tropomyosin的广泛相互作用.
- 这种复杂的绑定建议在尖端进行受监管的子单位交换的模型.
- 了解Tmod的结构为细胞骨调节提供了洞察力.
相关概念视频
Actin Polymerization
6.3K
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...
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...
6.3K
Mechanism of Filopodia Formation
2.4K
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...
2.4K
Actin Filament Depolymerization
3.0K
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...
3.0K
Generation of Straight or Branched Actin Filaments
2.9K
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...
2.9K
Mechanism of Lamellipodia Formation
3.1K
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...
3.1K
Actin Treadmilling
7.9K
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...
7.9K


