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相关概念视频

Actin Treadmilling01:18

Actin Treadmilling

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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...
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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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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...
2.9K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

3.1K
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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Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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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....
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The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

3.5K
Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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相关实验视频

Updated: Jul 16, 2025

Tuning the Contractility and Deformation Modes of Active Actin-Based Assemblies In Vitro: From Two-Dimensional Active Networks to Liquid Crystal Drops
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摩擦模式指导着活动网络的收缩.

Alexandra Colin1, Magali Orhant-Prioux1, Christophe Guérin1

  • 1Université Grenoble-Alpes, CEA, CNRS, UMR5168, Interdisciplinary Research Institute of Grenoble, CytoMorpho Lab, Grenoble 38054, France.

Proceedings of the National Academy of Sciences of the United States of America
|September 19, 2023
PubMed
概括
此摘要是机器生成的。

细胞形状取决于内部的actomyosin力量和外部摩擦. 这项研究表明摩擦力显著直接作用于actin网络收缩,影响细胞变形.

关键词:
这就是Actin Actin.收缩的收缩 收缩的收缩细胞骨架 细胞骨架摩擦摩擦 摩擦 摩擦

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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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The Mechanics of Poro-Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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The Mechanics of Poro-Elastic Contractile Actomyosin Networks As a Model System of the Cell Cytoskeleton
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科学领域:

  • 生物物理学的生物物理.
  • 细胞生物学 细胞生物学
  • 材料科学 材料科学 材料科学

背景情况:

  • 细胞形状是由内部的actomyosin力和外部的电阻力决定的.
  • 在活细胞中解开收缩,定和摩擦力是具有挑战性的.

研究的目的:

  • 在实验室中研究摩擦力在actomyosin网络变形中的特定作用.
  • 了解摩擦大小和分布如何影响网络收缩.

主要方法:

  • 在微型玻璃和脂质表面上重建可收缩的actomyosin网络.
  • 通过不同的表面特性和微型模式调节摩擦力.
  • 诱导阿克丁网络组装和观察肌诱导的收缩.

主要成果:

  • 在脂质二层 (较低的摩擦力) 上,动氨酸网络变形的速度更快,更协调,而不是在玻璃上 (较高的摩擦力).
  • 不同质的微型图案显示偏向变形向摩擦较高的区域.
  • 摩擦模式强烈推动了网络收缩,覆盖了肌肉素分布效应.

结论:

  • 摩擦力在收缩期间指导actomyosin网络变形方面发挥着至关重要的作用.
  • 活性 (actomyosin) 和电阻 (摩擦) 两种力量都对控制细胞变形至关重要.
  • 这项工作提供了关于细胞形状和行为的机械调节的见解.