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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.
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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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Introduction to Actin01:26

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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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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.
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 Filament Depolymerization01:19

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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).
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Tension Response at Adherens Junctions01:26

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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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Measuring Protein Binding to F-actin by Co-sedimentation
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Alpha-actinin binding kinetics modulate cellular dynamics and force generation.

Allen J Ehrlicher1, Ramaswamy Krishnan2, Ming Guo3

  • 1Division of Nephrology, Department of Medicine, and School of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138; and Department of Bioengineering, McGill University, Montreal, QC, Canada H3A0C3 mpollak@bidmc.harvard.edu allen.ehrlicher@gmail.com.

Proceedings of the National Academy of Sciences of the United States of America
|April 29, 2015
PubMed
Summary
This summary is machine-generated.

Altered binding affinity of the actin cross-linker alpha-actinin 4 (ACTN4) in cells reduces cell movement but increases cellular forces. This suggests physical defects in the cytoskeleton can cause human diseases like kidney disease.

Keywords:
Alpha-actininactincell mechanicskidney diseasetraction force

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Area of Science:

  • Cell Biology
  • Biophysics
  • Biochemistry

Background:

  • The actin cytoskeleton is crucial for cell structure and motility, regulated by accessory proteins.
  • Actin cross-linking proteins form networks from filaments; their binding affinity's effect on cellular forces is poorly understood.

Purpose of the Study:

  • To investigate how the binding affinity of alpha-actinin 4 (ACTN4) affects cellular dynamics and forces within cells.
  • To explore the link between ACTN4 mutations, cellular mechanics, and human kidney disease.

Main Methods:

  • Fluorescence recovery after photobleaching (FRAP) to measure ACTN4 binding affinity to F-actin in cells.
  • Intracellular microsphere tracking to assess cytoplasmic mobility.
  • Traction force microscopy (TFM) to quantify cellular forces.

Main Results:

  • A kidney disease-associated ACTN4 mutation tripled binding affinity, increasing F-actin dissociation time.
  • Increased ACTN4 affinity reduced cytoplasmic mobility and halved cell speed.
  • Cells with higher ACTN4 affinity exhibited increased contractile stress and strain energy.

Conclusions:

  • Actin cross-linker binding affinity significantly impacts cellular mechanics, including mobility and force generation.
  • Altered cytoskeletal properties due to cross-linker mutations may underlie human diseases.
  • Cytoskeletal solid-like behavior and myosin activity partitioning are potential mechanisms for observed force changes.