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Related Concept Videos

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...
3.1K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

2.9K
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
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.3K
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...
2.3K
Actin Polymerization01:42

Actin Polymerization

6.5K
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...
6.5K
Destabilization of Microtubules01:45

Destabilization of Microtubules

2.7K
The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
2.7K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

19.4K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
19.4K

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Leiomodin 2 functions as a processive pointed-end elongator of actin filaments.

bioRxiv : the preprint server for biologyยท2026
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Twinfilin modulates tissue contractility through uncapping of capping protein in C. elegans.

Development (Cambridge, England)ยท2025
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A generalized theoretical framework to investigate multicomponent actin dynamics.

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Twinfilin is a potent uncapper of actin capping protein and modulates actomyosin contractility in the <i>C. elegans</i> spermatheca.

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Twinfilin is a nonprocessive depolymerase which synergizes with formin to dramatically accelerate actin filament uncapping by 300-fold.

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The actin filament pointed-end depolymerase Srv2/CAP depolymerizes barbed ends, displaces capping protein, and promotes formin processivity.

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Related Experiment Video

Updated: Jun 24, 2025

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

Published on: May 5, 2022

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Profilin affects microtubule dynamics via actin.

Heidi Ulrichs1, Shashank Shekhar1

  • 1Departments of Physics, Cell Biology and Biochemistry, Emory University, Atlanta, GA, USA.

The Journal of Cell Biology
|June 4, 2024
PubMed
Summary

Profilin

Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics

Background:

  • Profilin is known to bind microtubules in laboratory settings.
  • Its role in regulating microtubule dynamics within living cells remains less clear.

Purpose of the Study:

  • To investigate the in vivo effects of profilin on microtubule dynamics.
  • To determine if profilin's influence on microtubules is direct or indirect.

Main Methods:

  • The study utilized advanced cell imaging techniques.
  • Investigated the interplay between profilin, actin, and microtubules in cellular environments.

Main Results:

  • Profilin's observed effects on microtubule dynamics in cells are indirect.
  • These effects stem from profilin's well-established role in regulating actin dynamics.

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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence TIRF Microscopy
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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence TIRF Microscopy

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Reconstitution of Actin-Based Motility with Commercially Available Proteins

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Related Experiment Videos

Last Updated: Jun 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

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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence TIRF Microscopy
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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence TIRF Microscopy

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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Reconstitution of Actin-Based Motility with Commercially Available Proteins

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Conclusions:

  • Profilin does not directly regulate microtubule dynamics in cells.
  • Actin dynamics mediate profilin's indirect influence on the microtubule cytoskeleton.