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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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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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Mechanism of Filopodia Formation01:39

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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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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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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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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Formins specify membrane patterns generated by propagating actin waves.

Mary Ecke1, Jana Prassler1, Patrick Tanribil1

  • 1Max Planck Institute of Biochemistry, D-82152 Martinsried, Munich, Germany.

Molecular Biology of the Cell
|January 16, 2020
PubMed
Summary
This summary is machine-generated.

Circular actin waves create distinct cell surface areas. Formins, actin-associated proteins, specify these regions, influencing cell dynamics and membrane composition.

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Area of Science:

  • Cell biology
  • Biophysics

Background:

  • Circular actin waves delineate distinct regions on the cell surface.
  • These regions exhibit differences in protein and phosphoinositide composition.
  • The wave dynamics involve interconversion between these areas.

Purpose of the Study:

  • To investigate the role of formins in specifying cellular domains defined by actin waves.
  • To understand the spatial distribution and function of formins within the actin wave pattern.
  • To explore the contribution of formins to the generation and maintenance of these cellular territories.

Main Methods:

  • Photo-conversion of Eos-actin to analyze actin network turnover.
  • Total Internal Reflection Fluorescence (TIRF) microscopy to visualize formin localization.
  • Utilizing constitutively active formin constructs tagged with fluorescent proteins.
  • Employing the formin inhibitor SMIFH2 to assess formin involvement.

Main Results:

  • Actin networks exhibit continuous turnover in both inner and external territories.
  • Specific formins (ForB, ForG, ForA, ForE, ForH) show distinct localization patterns within the wave landscape.
  • ForB associates with the actin wave, ForG with the inner territory, and ForA, ForE, ForH with the external area.
  • Formin B (ForB) membrane binding fluctuations suggest transient domain states.
  • Inhibition of formins with SMIFH2 disrupts the actin wave patterns.

Conclusions:

  • Formins play a crucial role in specifying distinct membrane domains within the actin wave pattern.
  • The differential recruitment of formins contributes to the organization and maintenance of cellular territories.
  • Formins are implicated in the generation of circular actin wave patterns and associated domain differentiation.