Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

3.0K
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...
3.0K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.0K
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...
3.0K
Actin Polymerization01:42

Actin Polymerization

6.8K
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...
2.4K

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Red blood cell distribution width to albumin ratio and systemic immune-inflammatory index as predictors of mortality in severe pneumonia: A retrospective cohort analysis.

PloS one·2026
Same author

Wedelactone-loaded exosomes for sepsis-induced liver injury: a novel therapeutic strategy.

Drug delivery·2026
Same author

Targeting the crosstalk between Alzheimer's disease and gastrointestinal cancers.

Molecular medicine (Cambridge, Mass.)·2026
Same author

The anti-respiratory syncytial virus activity of biochemicals from Pyrola incarnata.

Antiviral research·2026
Same author

A Field-Deployable Microfluidic CNT-FET Platform for Direct Monitoring of Multiplexed Respiratory Viruses in Environmental Waters.

ACS sensors·2026
Same author

tRF and gastric cancer: molecular mechanism exploration and novel strategies for precision diagnosis and therapy.

Journal of translational medicine·2026

関連する実験動画

Updated: Aug 24, 2025

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

2.7K

F-アクチンの構造を調節する屈折力とヌクレオチド状態

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

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

Nature
|October 26, 2022
PubMed
まとめ

アクチンフィラメント (F-アクチン) のニュクレオチドの状態は,曲げられたときにその構造に影響します. リン酸の存在はアクチンを硬化させ,その機械的調節を変化させ,アクチン結合タンパク質を誘導する可能性がある.

さらに関連する動画

Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

1.8K
Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones
09:14

Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones

Published on: March 17, 2011

14.9K

関連する実験動画

Last Updated: Aug 24, 2025

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

2.7K
Reconstitution of Actin-Based Motility with Commercially Available Proteins
08:40

Reconstitution of Actin-Based Motility with Commercially Available Proteins

Published on: October 28, 2022

1.8K
Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones
09:14

Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones

Published on: March 17, 2011

14.9K

科学分野:

  • 生物化学
  • 細胞生物学
  • 構造生物学

背景:

  • アクチンのポリメリゼーションは 細胞の力生成の鍵です
  • アクチンフィラメント (F-アクチン) の動態は,力とヌクレオチド状態によって制御されるが,そのメカニズムは不明である.

研究 の 目的:

  • アクチンヌクレオチド状態が折りたたみ力によるF-アクチン構造的移行をどのように調節するかを調査する.
  • F-アクチンの機械的調節におけるアクチンヌクレオチド状態の役割を解明する.

主な方法:

  • ADP-F-アクチンとADP-Pi-F-アクチンの構造を決定するための冷凍電子顕微鏡 (冷凍-EM).
  • 高解像度でF-アクチンの構造を再構築するための 機械学習パイプライン
  • サブユニット間のインターフェースと曲げられたフィラメントの形状の変化の分析.

主要な成果:

  • ADP-F-actinとADP-Pi-F-actinの格子は,低解像度でほとんど同じで,バックボンの違いは最小です.
  • 曲げられたF-アクチンの構造は,変化した螺旋状の回転とプロトメアの変形を含む,サブユニット間のインターフェイスで明確な再配置を明らかにする.
  • フォスファートはアクチンのサブユニットを硬化させ 曲げられた構造に影響を及ぼします

結論:

  • アクチンヌクレオチド状態は,F-アクチンの屈折力に対する反応を大きく調節する.
  • 曲げられたF-アクチンのコンフォームトランジションはヌクレオチド状態に依存し,アクチン結合タンパク質によって検出できるほど大きい.
  • アクチンヌクレオチド状態は,F-アクチンの機械的性質の共同調節剤として作用する.