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相关概念视频

Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

2.9K
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...
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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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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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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.3K
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...
2.3K
Actin Polymerization01:42

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...
6.3K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

5.1K
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....
5.1K
Actin Filament Depolymerization01:19

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...
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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的结构性可塑性介导了灵活的活性束结构.

Rui Gong1, Matthew J Reynolds2, Keith R Carney3,4

  • 1Laboratory of Structural Biophysics and Mechanobiology, The Rockefeller University, New York, NY, USA. rgong@rockefeller.edu.

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概括

素蛋白形成了细胞结构必不可少的活性丝束. 向法斯的抑制剂通过阻断其F-actin交叉链接机制,显示出对癌症治疗的希望.

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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:

  • 素是一种关键的活性蛋白结合蛋白,它将活性纤维 (F-actin) 交叉结合成捆.
  • 这些捆绑对细胞结构至关重要,如filopodia和stereocilia.
  • 发酵因子的失调有助于癌症转移,使其成为治疗点.

研究的目的:

  • 在各种尺度上阐明人类fascin-1的F-actin交叉链接机制.
  • 了解fascin-1是如何构建和调节actin捆的.
  • 为了研究 Fascin 抑制剂活性的结构基础.

主要方法:

  • 低温电子显微镜 (cryo-EM) 和低温电子断层扫描 (cryo-ET).
  • 定制拒绝算法和计算建模.
  • 对fascin-actin交叉桥梁和线束的结构分析.

主要成果:

  • 确定了fascin. 的不对称F-actin结合形状.
  • 确定G2抑制剂以全性方式阻断这种结合部位.
  • 揭示了法斯的结构可塑性,使其能够适应各种F-actin方向.
  • 揭露了管理迷人的绑定模式和捆绑大小限制的几何规则.

结论:

  • Fascin利用纳米尺度的结构动力学来构建和控制微米尺度的活性束.
  • 了解法斯的机制,可以了解它在细胞迁移和转移中的作用.
  • 这些结构性发现支持开发基于魅力的癌症治疗方法.