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Related Concept Videos

Generation of Straight or Branched Actin Filaments01:14

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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.
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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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Mechanism of Lamellipodia Formation01:31

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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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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
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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.
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Related Experiment Video

Updated: Jul 21, 2025

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Multi-monoubiquitination 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.

Biorxiv : the Preprint Server for Biology
|July 28, 2023
PubMed
Summary
This summary is machine-generated.

Ubiquitination of the actin regulator VASP was found to negatively impact its interaction with actin filaments, affecting cell shape. This study reveals how ubiquitination controls VASP-mediated actin dynamics.

Keywords:
VASPactinubiquitination

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Area of Science:

  • Cell Biology
  • Cytoskeleton Dynamics
  • Protein Regulation

Background:

  • The actin cytoskeleton is crucial for cellular functions, necessitating tight regulation of actin polymerization.
  • Previous work showed reversible ubiquitination regulates the actin polymerase VASP in neurons, but the mechanism was unclear.

Approach:

  • Mimicked multi-monoubiquitination of VASP at specific sites (K240, K286).
  • Utilized in vitro biochemical assays to assess VASP-actin interactions.
  • Introduced recombinant multi-monoubiquitinated VASP into cells to observe morphological changes.

Key Points:

  • Multi-monoubiquitination at K240 and K286 negatively regulates VASP's interaction with actin.
  • Ubiquitinated VASP showed reduced ability to bind, bundle, and elongate actin filaments.
  • Ubiquitinated VASP retained the capacity to bind and protect actin barbed ends from capping protein.

Conclusions:

  • Ubiquitination directly impacts VASP's function in regulating actin dynamics.
  • This provides a molecular mechanism for how ubiquitination controls VASP activity.
  • The findings offer insights into the cellular control of actin polymerization and cell morphology.