Actin Microtubule Mixtures
Actin Microtubule Mixtures - Related Videos
07:27
TIRF Microscopy to Visualize Actin and Microtubule Coupling Dynamics
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2025
This video describes TIRF, a total internal reflection microscopy-based technique to visualize actin and microtubule polymerization dynamics. The method allows the high-resolution imaging of actin and microtubule coupling dynamics in real-time, which is essential for understanding cellular crosstalks.
12:20
Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
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Cited by 24 •
2014
Microtubules are inherently unstable polymers, and their switching between growth and shortening is stochastic and difficult to control. Here we describe protocols using segmented microtubules with photoablatable stabilizing caps. Depolymerization of segmented microtubules can be triggered with high temporal and spatial resolution, thereby assisting analysis of motions with the disassembling microtubule ends.
10:13
Quantification of Filamentous Actin (F-actin) Puncta in Rat Cortical Neurons
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Cited by 8 •
2016
Filamentous actin (F-actin) plays an important role in spinogenesis, synaptic plasticity, and synaptic stability. Quantification of F-actin puncta is therefore a useful tool to study the integrity of synaptic structures. This protocol describes the procedures of quantifying F-actin puncta labeled with Phalloidin in low-density primary cortical neuronal cultures.
03:27
Mixtures of Acids
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2020
The pH of a solution containing an acid can be determined using its acid dissociation constant and its initial concentration. If a solution contains two different acids, then its pH can be determined using one of several methods depending upon the relative strength of the acids and their dissociation constants. A Mixture of a Strong Acid and a Weak Acid In a mixture of a strong acid and a weak acid, the strong acid dissociates completely and becomes a source of almost all the hydronium ions...
06:17
Measuring Protein Binding to F-actin by Co-sedimentation
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Cited by 18 •
2017
This protocol describes a method to test the ability of a protein to co-sediment with filamentous actin (F-actin) and, if binding is observed, to measure the affinity of the interaction.
FAQs
Their interaction can arise through steric forces, which result from physical crowding, as well as through cross-linking proteins and motor activity. These connections allow the two polymer systems to affect one another’s organization without requiring them to become the same structure. Reconstituted mixtures therefore provide a way to examine how separate cytoskeletal components cooperate mechanically.
Changing filament concentration alters how frequently the polymers encounter one another, while network connectivity determines how effectively forces and structural constraints can extend through the composite. Filament dynamics add another source of variation by changing network organization over time. Together, these variables can shift the mixture’s structure and mechanical behavior, making them important experimental control parameters.
Motor activity provides a mechanism that can actively influence the arrangement and behavior of the actin and microtubule networks. Its effects can be considered alongside passive steric interactions and protein-mediated cross-linking, allowing researchers to distinguish how active and structural interactions contribute to organization. This distinction connects the mixtures to broader studies of active matter and cellular mechanics.
Researchers assemble the two polymer networks in a controlled assay and vary factors such as filament concentration, network connectivity, dynamics, cross-linking, or motor activity. They then examine resulting changes in organization and mechanical behavior. This reduction of cellular complexity makes it possible to test how selected components and conditions influence the composite system without treating the entire cell as an uncontrolled experimental environment.
These systems are useful when the goal is to investigate cooperation between cytoskeletal networks in cell shape regulation, intracellular transport, division, or migration. Because the actin and microtubule components can be examined together, the assays help connect physical interactions between polymers with broader cellular processes. They also offer a controllable context for exploring how cytoskeletal organization supports changing cell behaviors.
Beyond specific cellular processes, the mixtures serve as controllable models of active matter and biomolecular materials. Their responses to changes in polymer concentration, dynamics, connectivity, and motor activity can reveal physical principles underlying cellular organization. The resulting observations help relate molecular components to emergent material properties, including the structure and mechanical behavior of composite cytoskeletal networks.