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Related Concept Videos

Cytoskeletal Proteins in Bacteria01:29

Cytoskeletal Proteins in Bacteria

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Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
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Introduction to Actin01:26

Introduction to Actin

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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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Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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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.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
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Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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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.
The high-order actin...
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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 Polymerization01:42

Actin Polymerization

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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.
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...
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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Actin: Structure, Function, Dynamics, and Interactions with Bacterial Toxins.

Sonja Kühn1, Hans Georg Mannherz2

  • 1Department of Cell Biology and Infection, Institut Pasteur, Paris, France.

Current Topics in Microbiology and Immunology
|November 17, 2016
PubMed
Summary
This summary is machine-generated.

Actin, a key cytoskeletal protein, forms filaments essential for cell structure and movement. Bacterial toxins target actin to manipulate host cells for their own needs.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Actin is a highly abundant eukaryotic protein crucial for cytoskeleton structure and function.
  • Six conserved actin isoforms exist in mammals, differing slightly in amino acid sequences.
  • Actin filaments stabilize cell shape and drive motile activities like vesicle transport and cell locomotion.

Purpose of the Study:

  • To describe the structure of monomeric and polymeric actin.
  • To elucidate actin polymerization kinetics.
  • To explain the regulation of actin by actin-binding proteins.

Main Methods:

  • Structural analysis of actin monomers and polymers.
  • Kinetic studies of actin polymerization.
  • Investigation of actin regulation by associated proteins.

Main Results:

  • Detailed description of monomeric and polymeric actin structures.
  • Characterization of actin polymerization dynamics.
  • Identification of key actin-binding proteins regulating filament formation and function.

Conclusions:

  • Actin's fundamental role in eukaryotic cell biology is highlighted.
  • Actin polymerization and its regulation are complex processes.
  • Bacterial toxins exploit the host actin cytoskeleton for their advantage.