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Related Concept Videos

Actin Treadmilling01:18

Actin Treadmilling

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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
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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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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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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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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).
In F-actin, the ADF/cofilin proteins...
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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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The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones
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Remodeling of the Actin/Spectrin Membrane-associated Periodic Skeleton, Growth Cone Collapse and F-Actin Decrease

Nicolas Unsain1,2, Martin D Bordenave3, Gaby F Martinez4,5

  • 1Instituto de Investigación Médica Mercedes y Martín Ferreyra, INIMEC-Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), UNC, Friuli, 2434 - 5016, Córdoba, Argentina. nunsain@immf.uncor.edu.

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Summary

Axonal degeneration involves actin cytoskeleton changes. Stabilizing actin prevents axon fragmentation, indicating the membrane-associated periodic skeleton

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Developmental Biology

Background:

  • Axonal degeneration is crucial for nervous system development and implicated in neurodegenerative diseases.
  • The role of the cytoskeleton, particularly actin, during axonal degeneration remains poorly understood.

Purpose of the Study:

  • To investigate the changes and role of the actin cytoskeleton during axonal degeneration using an in vitro model.

Main Methods:

  • Utilized an in vitro model of developmental axonal pruning induced by trophic factor withdrawal (TFW).
  • Employed super-resolution STED microscopy to analyze the actin/spectrin membrane-associated periodic skeleton (MPS).
  • Assessed the impact of pharmacological actin stabilizers on axonal fragmentation.

Main Results:

  • Trophic factor withdrawal led to early F-actin decrease and growth cone collapse (GCC), independent of fragmentation.
  • Super-resolution microscopy revealed a significant loss and disorganization of the axonal MPS shortly after TFW.
  • Fragmented axons lacked MPS, while microtubule integrity was maintained.
  • Pharmacological stabilization of actin filaments prevented MPS loss and protected axons from fragmentation.

Conclusions:

  • Axonal degeneration involves distinct pathways for growth cone collapse and fragmentation.
  • The membrane-associated periodic skeleton (MPS) is essential for axonal integrity.
  • Destruction of the MPS is a required step for axonal fragmentation during degeneration.