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Related Concept Videos

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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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 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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Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Adaptability of Cytoskeletal Filaments01:12

Adaptability of Cytoskeletal Filaments

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The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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The evolution of compositionally and functionally distinct actin filaments.

Peter W Gunning1, Umesh Ghoshdastider2, Shane Whitaker1

  • 1School of Medical Sciences, University of New South Wales, Sydney, NSW, 2052, Australia.

Journal of Cell Science
|March 20, 2015
PubMed
Summary

Actin filaments are highly conserved in eukaryotes but diverse in bacteria. Evolutionary pressures led to varied actin compositions across kingdoms, expanding functional diversity through different mechanisms in bacteria, plants, and animals.

Keywords:
ActinEvolutionFilamentTropomyosin

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Area of Science:

  • Evolutionary biology
  • Cell biology
  • Biochemistry

Background:

  • Actin filaments are fundamental cellular structures conserved across eukaryotes for billions of years.
  • Bacterial actin-like proteins show extreme divergence, making them difficult to identify via sequence homology.
  • Eukaryotic actin acts as a universal force provider, while bacteria employ a one-filament-one-function system.

Purpose of the Study:

  • To investigate the evolutionary diversification of actin filament composition across different kingdoms.
  • To understand the mechanisms driving functional expansion of actin-based systems.

Main Methods:

  • Phylogenetic analyses were employed to trace the evolutionary history of actin and related proteins.
  • Comparative analysis of gene expansion in plants and tropomyosin diversification in fungi and metazoa.

Main Results:

  • Phylogenetic analyses reveal an evolutionary drive for actin filament compositional diversity across kingdoms.
  • Bacteria utilize distinct filament systems for specialized functions.
  • Eukaryotes, specifically plants, show gene expansion, while fungi and metazoa exhibit tropomyosin diversification to enhance actin filament variety.

Conclusions:

  • Different evolutionary strategies, including gene expansion and protein diversification, have led to varied actin filament compositions across bacteria, plants, and metazoa.
  • This compositional variation enables specialized functions and expands the functional repertoire of actin-based systems in diverse organisms.