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Related Concept Videos

Actin Polymerization01:42

Actin Polymerization

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 actin...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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...
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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 networks...
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.

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Updated: Jun 7, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

Dynamin architecture--from monomer to polymer.

Harry H Low1, Jan Löwe

  • 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom. h.low@mail.cryst.bbk.ac.uk

Current Opinion in Structural Biology
|October 26, 2010
PubMed
Summary
This summary is machine-generated.

Dynamins, proteins crucial for membrane dynamics, exhibit a conserved structural fold across species. Recent data reveals a unified model of dynamin architecture, challenging traditional domain divisions.

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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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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
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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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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

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Dynamins are essential proteins involved in membrane remodeling processes like fission and fusion.
  • Their complex self-assembly mechanisms are linked to lipid bilayer tubulation and destabilization.
  • Understanding dynamin function requires detailed insights into their structure at various assembly states.

Purpose of the Study:

  • To present a unified model of dynamin architecture.
  • To integrate recent structural data with existing knowledge of dynamin function.
  • To challenge traditional domain classifications based on new structural evidence.

Main Methods:

  • Analysis of recent high-resolution structural data of dynamins.
  • Comparison of structural data across different dynamin families and kingdoms.
  • Integration of structural findings with biochemical and sequence-based information.

Main Results:

  • Recent structural data provides detailed insights into dynamin assembly, from monomers to polymers.
  • A conserved basic dynamin fold is observed across eukaryotic and prokaryotic proteins.
  • Traditional divisions of dynamin subunits (GTPase, middle, and GTPase effector domains) are not supported by structural data.

Conclusions:

  • A unified model of dynamin architecture is proposed, emphasizing a conserved fold.
  • This model reconciles structural observations with the diverse functions of dynamins.
  • The findings necessitate a re-evaluation of dynamin domain organization and evolutionary relationships.