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Related Concept Videos

Introduction to Actin01:26

Introduction to Actin

6.9K
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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Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

4.0K
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...
4.0K
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

7.0K
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....
7.0K
Actin Polymerization01:42

Actin Polymerization

8.9K
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...
8.9K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

4.1K
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...
4.1K
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

3.8K
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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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Exploring the A22-Bacterial Actin MreB Interaction through Molecular Dynamics Simulations.

Yaw Awuni1, Shimin Jiang2, Robert C Robinson1,2,3,4,5

  • 1School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive, Singapore 637551.

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The antibiotic A22 perturbs bacterial MreB protein function by affecting ATP release, not hydrolysis. This finding aids in designing new MreB inhibitors for bacterial shape control.

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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence TIRF Microscopy
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Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
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Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence TIRF Microscopy
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Area of Science:

  • Bacterial cytoskeleton dynamics
  • Molecular mechanisms of antibiotic action

Background:

  • MreB protein maintains bacterial rod shape.
  • Antibiotic A22 disrupts MreB function and cell morphology.
  • A22's precise inhibition mechanism on MreB's ATP hydrolysis remains unclear.

Purpose of the Study:

  • To elucidate the mechanism by which A22 inhibits MreB.
  • To investigate the structural and dynamic interactions of MreB with A22 and nucleotides.

Main Methods:

  • Conventional molecular dynamics simulations.
  • Analysis of MreB active site dynamics in complex with A22 and nucleotides.
  • Water dynamics analysis in the MreB active site.

Main Results:

  • Hydrogen bonding between A22 and Glu140 is disfavored in the ATP-A22-bound state.
  • A22 allows water molecules to occupy positions conducive to ATP hydrolysis.
  • A22 appears to slow phosphate release from MreB.

Conclusions:

  • A22 inhibits MreB by affecting polymerization/depolymerization dynamics, primarily by slowing phosphate release.
  • The findings provide insights into A22's mechanism of action.
  • Data can inform the development of novel MreB inhibitors.