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Related Concept Videos

Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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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...
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Actin Filament Depolymerization01:19

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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...
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Actin Polymerization01:42

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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.
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Actin Polymerization and Cell Motility01:13

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Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
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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...
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Introduction to Actin01:26

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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...
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Related Experiment Video

Updated: Jul 4, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Multi-monoubiquitylation controls VASP-mediated actin dynamics.

Laura E McCormick1, Cristian Suarez2,3, Laura E Herring4,5

  • 1Department of Cell Biology and Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Journal of Cell Science
|January 26, 2024
PubMed
Summary

Ubiquitylation of the actin regulator VASP at specific sites negatively impacts its interaction with actin filaments. This regulation controls VASP-mediated actin dynamics, crucial for cellular functions.

Keywords:
ActinFilopodiaNondegradativeTRIM9UbiquitylationVASP

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • The actin cytoskeleton is vital for cellular functions and requires tight regulation of actin polymerization.
  • Reversible, non-degradative ubiquitylation was previously shown to regulate the actin polymerase VASP in developing neurons.
  • The precise mechanism by which ubiquitylation affects VASP activity remained unclear.

Purpose of the Study:

  • To elucidate the mechanism by which ubiquitylation impacts VASP activity and its interaction with actin.
  • To investigate the functional consequences of VASP ubiquitylation on actin dynamics.

Main Methods:

  • Mimicking multi-monoubiquitylation of VASP at specific lysine residues (K240 and K286).
  • In vitro biochemical assays to assess VASP's binding, bundling, and elongation of actin filaments.
  • Electroporation of recombinant multi-monoubiquitylated VASP protein into cells to observe morphological changes.

Main Results:

  • Mimicking VASP ubiquitylation at K240 and K286 negatively regulated its interaction with actin.
  • Multi-monoubiquitylated VASP showed reduced ability to bind, bundle, and elongate actin filaments in vitro.
  • Ubiquitylated VASP retained its capacity to bind and protect barbed ends from capping protein.
  • Electroporation of ubiquitylated VASP altered cell spreading morphology.

Conclusions:

  • Ubiquitylation acts as a regulatory mechanism controlling VASP's interaction with actin.
  • This ubiquitylation-mediated regulation influences VASP's role in actin dynamics.
  • The findings provide a mechanistic link between ubiquitylation and the regulation of the actin cytoskeleton.