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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

3.6K
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...
3.6K
Introduction to Actin01:26

Introduction to Actin

6.2K
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...
6.2K
Actin Polymerization01:42

Actin Polymerization

8.2K
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...
8.2K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.5K
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...
3.5K
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

8.4K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
8.4K
Actin Treadmilling01:18

Actin Treadmilling

9.4K
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...
9.4K

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相关实验视频

Updated: Jan 7, 2026

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
06:48

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops

Published on: July 11, 2025

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通过多尺度增强采样显示的核酸依赖性actin形状.

Kenta Omoto1, Ryotaro Koike2, Kei Moritsugu1

  • 1Graduate School of Science, Osaka Metropolitan University, 1-2 Gakuencho, Naka-ku, Sakai, Osaka 599-8570, Japan.

Biophysical journal
|December 7, 2025
PubMed
概括

由于核酸结合,动氨酸丝的生长是定向的. 与ATP结合的动因单体有利于刺末端的添加,而与ADP结合的动因则有利于尖端的解离,解释了线程极性.

科学领域:

  • 生物化学 生物化学
  • 细胞生物学 细胞生物学
  • 生物物理学的生物物理.

背景情况:

  • 动氨酸丝形成细胞骨架,对细胞运动和运输至关重要.
  • 导线极性 (有刺的/加点和尖的/减点的末端) 决定了成长的方向.
  • 核酸状态 (ATP与ADP对比) 调节了actin的动态.

研究的目的:

  • 研究G-actin和F-actin与结合的ATP或ADP的结构动态.
  • 阐明了核酸依赖性actin丝的极性和生长背后的分子机制.

主要方法:

  • 多尺度增强采样模拟用于构造分析.
  • 采用了高分辨率的晶体结构的活性蛋白结合蛋白复合体.
  • 进行原子接触分析以确定关键相互作用.

主要成果:

  • 与ATP结合的G-actin表现出更大的灵活性,有利于丝协会.
  • 与ADP结合的F-actin表现出更大的灵活性,促进与尖端的解离.
  • 核酸依赖的形状变化解释了行为丝的方向生长.

结论:

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Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Reconstituting and Characterizing Actin-Microtubule Composites with Tunable Motor-Driven Dynamics and Mechanics
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  • 这项研究解释了基于核酸状态的行为丝的定向生长.
  • 结合ATP增强了G-actin连接线索刺尾的能力.
  • 通过ADP结合,促进F-actin与丝尖端的解离.