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相关概念视频

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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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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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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Actin Polymerization01:42

Actin Polymerization

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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...
6.8K
Introduction to Actin01:26

Introduction to Actin

5.3K
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...
5.3K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.2K
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...
3.2K
Mechanism of Filopodia Formation01:39

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...
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曲力和核酸状态共同调节F-actin结构

Matthew J Reynolds1, Carla Hachicho1, Ayala G Carl1,2

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

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PubMed
概括

动氨酸丝 (F-actin) 核酸状态会影响其曲时的结构. 酸盐的存在使动蛋白变硬,改变机械调节,并可能引导动蛋白结合蛋白.

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科学领域:

  • 生物化学
  • 细胞生物学
  • 结构生物学

背景情况:

  • 动蛋白聚合是细胞力量生成的关键.
  • 乙丝 (F-乙) 的动态受力和核酸状态的调节,但机制尚不清楚.

研究的目的:

  • 研究如何在曲力下调节F-actin结构过渡.
  • 阐明在F-actin的机械调节中的actin核酸状态的作用.

主要方法:

  • 电子显微镜 (cryo-EM) 用于确定ADP-F-actin和ADP-Pi-F-actin的结构.
  • 用于高分辨率重建曲的F-actin结构的机器学习管道.
  • 曲线线的子单位间接口和形状变化的分析.

主要成果:

  • 在低分辨率下,ADP-F-actin和ADP-Pi-F-actin网格几乎相同,骨干差异很小.
  • 曲的F-actin结构显示在子单元之间的界面有明显的重排,包括改变的螺旋扭曲和原体变形.
  • 酸盐似乎会使动素子单元变硬,从而影响曲的结构格局.

结论:

  • 乙核酸状态显著调节F-乙对曲力的反应.
  • 曲F-actin中的形态转换依赖于核酸状态,并且足以被actin结合蛋白检测.
  • 乙核酸状态作为F-乙机械性质的共同调节者.