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Related Concept Videos

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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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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The Nucleolus02:55

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The nucleolus is the most prominent substructure of the nucleus. When it was first discovered, it was considered to be an isolated organelle that forms fibrils and granules. In 1931, the relationship between the nucleolus and chromosomes was first described by Heitz. He observed that the appearance and size of nucleolus varies depending on the stage of the cell cycle. He also noticed constricted regions on different chromosomes clustered together at definite cell cycle stages. These regions,...
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Ribosomal RNA Synthesis02:53

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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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Formation of Higher-order Actin Filaments01:11

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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.
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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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In Vitro Polymerization of F-actin on Early Endosomes
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Partitioning of ribonucleoprotein complexes from the cellular actin cortex.

Isaac Angert1,2,3, Siddarth Reddy Karuka1, Louis M Mansky2,3,4

  • 1School of Physics and Astronomy, University of Minnesota, Minneapolis, MN 55455, USA.

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The actin cortex helps organize cell contents. Researchers found RNA binding proteins are excluded from the cell cortex, suggesting the cortex regulates biomolecule distribution near the cell membrane.

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Area of Science:

  • Cell Biology
  • Biophysics

Background:

  • The cell cortex, a meshwork of proteins beneath the plasma membrane, is vital for cell mechanics and signaling.
  • Its influence on the spatial distribution of intracellular biomolecules remains largely unknown.

Purpose of the Study:

  • To investigate how the cell cortex affects the distribution of cytoplasmic biomolecules.
  • To develop a method for accurately mapping biomolecule distribution within cells.

Main Methods:

  • Developed a super-resolution fluorescence microscopy technique to visualize biomolecule distribution.
  • Performed diffusion measurements on RNA-protein complexes.

Main Results:

  • RNA binding proteins were found to be partially excluded from the cell cortex region.
  • Excluded volume interactions could explain this observed partitioning of RNA binding proteins.

Conclusions:

  • The actin cortex meshwork may play a role in regulating the composition of the cytoplasm near the plasma membrane.
  • This finding offers insights into the spatial organization of cellular components.