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Related Concept Videos

Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
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...
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...
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...

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DNA Nanotubes as a Versatile Tool to Study Semiflexible Polymers
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Pattern-induced thermal unbinding of filaments.

O Pierre-Louis1

  • 1LPMCN, Université Lyon 1, Villeurbane, France.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics
|March 17, 2011
PubMed
Summary

Substrate patterning offers a novel way to control filament adhesion and observe unbinding transitions. This method facilitates easier observation of unbinding phenomena compared to flat surfaces.

Area of Science:

  • Physics
  • Materials Science
  • Surface Science

Background:

  • Controlling the adhesion of filaments to surfaces is crucial in various scientific and industrial applications.
  • Understanding unbinding transitions is key to predicting material behavior under different conditions.

Purpose of the Study:

  • To investigate the use of substrate patterning for controlling filament adhesion.
  • To explore the characteristics of unbinding transitions on patterned substrates.
  • To determine the influence of transverse fluctuations and temperature on binding and unbinding phenomena.

Main Methods:

  • Utilizing patterned substrates to guide filament adhesion.
  • Analyzing the effects of temperature on filament unbinding.
  • Investigating the role of transverse fluctuations in the unbinding transition.

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

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Ensemble Force Spectroscopy by Shear Forces
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Ensemble Force Spectroscopy by Shear Forces

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

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Ensemble Force Spectroscopy by Shear Forces
07:30

Ensemble Force Spectroscopy by Shear Forces

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Main Results:

  • Substrate patterning effectively controls filament adhesion.
  • Unbinding transitions occur at finite temperatures on patterned substrates.
  • The dimensionality of transverse fluctuations dictates the transition's continuity.
  • Re-entrant binding is observed with increasing temperature in certain cases.
  • Unbinding is more readily observed on patterned surfaces than on flat substrates.

Conclusions:

  • Substrate patterning provides a facile method for controlling filament adhesion and studying unbinding transitions.
  • Patterned substrates offer advantages for observing unbinding phenomena compared to flat surfaces.
  • The study discusses experimental conditions for observing these unbinding phenomena.