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Related Concept Videos

Septins01:19

Septins

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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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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).
In F-actin, the ADF/cofilin proteins...
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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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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Role of Septins01:02

Role of Septins

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
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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.
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Related Experiment Video

Updated: May 27, 2025

Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution
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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

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Cdc42EP3-bound septin scaffolds promote actin polymerization.

Meagan R Tomasso1, Prajakta D Mehetre1, Priyashree Nagarajan1

  • 1Department of Biochemistry and Molecular Biology, Drexel University, Philadelphia, Pennsylvania, USA.

The Journal of Biological Chemistry
|February 19, 2025
PubMed
Summary

Cdc42EP3 protein directly binds septins and actin, promoting actin polymerization. This reveals Cdc42EP3 actively builds actin polymers on septin scaffolds, advancing cytoskeletal research.

Keywords:
CDC42Cdc42EP/BORGG-actinactinbundlingcytoskeletonfilament nucleationmicrofilamentsseptin

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Area of Science:

  • Cell Biology
  • Cytoskeletal Dynamics

Background:

  • Septins are cytoskeletal proteins crucial for cellular processes, often interacting with actin and microtubules.
  • The precise mechanisms by which septins contribute to actin- and microtubule-based functions remain incompletely understood.
  • Cdc42EP3 (BORG2) is known to recruit septins to actin structures, but its direct role in septin-actin interactions is unclear.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which Cdc42EP3 influences the interaction between septins and F-actin.
  • To determine if Cdc42EP3 directly binds septins and actin components.
  • To investigate the effect of Cdc42EP3 on actin polymerization in the presence of septins.

Main Methods:

  • Biochemical assays using purified proteins.
  • Analysis of binding interactions between Cdc42EP3, septins, and actin.
  • Monitoring of actin polymerization dynamics.

Main Results:

  • Cdc42EP3 directly binds to both septins and actin filaments.
  • Cdc42EP3 also interacts with individual actin monomers.
  • Septin-bound Cdc42EP3 significantly accelerates the polymerization of actin filaments.

Conclusions:

  • Cdc42EP3 acts as a direct mediator between septins and actin.
  • Cdc42EP3 is not just a crosslinking factor but actively promotes actin polymer formation on septin scaffolds.
  • This finding provides new insights into the regulation of cytoskeletal organization and dynamics by septin-associated proteins.