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Related Concept Videos

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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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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
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Formation of Higher-order Actin Filaments01:11

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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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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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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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VASP localization to lipid bilayers induces polymerization driven actin bundle formation.

T Nast-Kolb1, P Bleicher1,2, M Payr1,3

  • 1Lehrstuhl für Biophysik E27, Physik-Department, Technische Universität München, Garching, Germany and.

Molecular Biology of the Cell
|July 13, 2022
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Summary
This summary is machine-generated.

Vasodilator-stimulated phosphoprotein (VASP) binding to membranes drives actin bundle formation during polymerization. Membrane-bound VASP acts as both an actin elongator and bundler, influencing cytoskeleton structure.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Cytoskeleton Dynamics

Background:

  • Actin bundles are crucial for cellular force transmission and are formed by cross-linking proteins.
  • Vasodilator-stimulated phosphoprotein (VASP) is known as an actin elongator but also localizes to bundled actin structures.
  • The precise conditions under which VASP functions as an actin bundler versus an elongator remain unclear.

Purpose of the Study:

  • To investigate the role of membrane-bound VASP in actin bundle formation.
  • To elucidate the mechanism by which VASP transitions between actin elongation and bundling functions.
  • To understand how VASP localization influences its interaction with actin filaments and lipid bilayers.

Main Methods:

  • In vitro polymerization assays.
  • Observation of VASP behavior on fluid lipid bilayers during actin polymerization.
  • Analysis of VASP phase separation and its effect on actin bundle organization.

Main Results:

  • Membrane-bound VASP promotes the formation of large actin bundles during polymerization.
  • Lipid bilayer fluidity is essential for VASP-mediated actin alignment.
  • VASP undergoes phase separation on the bilayer, forming VASP-rich phases that nucleate and accumulate at actin bundles.
  • VASP captures and tracks growing actin filament barbed ends, facilitating bundling.

Conclusions:

  • VASP's localization dictates its function; membrane association enables bundling.
  • VASP acts as both an elongator and bundler simultaneously when concentrated during polymerization.
  • VASP-mediated actin bundling leads to the reorganization of the underlying lipid bilayer structure.