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Related Concept Videos

The Contractile Ring02:15

The Contractile Ring

Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
The Contractile Ring02:15

The Contractile Ring

Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
A small GTPase, RhoA, controls the function and assembly of the contractile ring. RhoA belongs to the Ras superfamily of proteins. The activation of formins by RhoA promotes...
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

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.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

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...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

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...
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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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Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast
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Actin depolymerization drives actomyosin ring contraction during budding yeast cytokinesis.

Inês Mendes Pinto1, Boris Rubinstein, Andrei Kucharavy

  • 1Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA.

Developmental Cell
|June 16, 2012
PubMed
Summary

Actin filament depolymerization is key to actomyosin ring constriction during cell division. This process, driven by actin depolymerization and myosin II, ensures consistent division timing regardless of cell size.

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Area of Science:

  • Cell biology
  • Cytokinesis research
  • Molecular mechanisms of cell division

Background:

  • Actin filaments and myosin II are essential for the contractile ring in cytokinesis.
  • Understanding the precise mechanisms driving actomyosin ring constriction is crucial for cell division research.

Purpose of the Study:

  • To investigate the role of actin filament depolymerization in actomyosin ring constriction during budding yeast cytokinesis.
  • To quantitatively model the contributions of actin depolymerization and myosin II motor activity to ring constriction.

Main Methods:

  • Utilized cofilin mutations and chemical stabilization to alter actin filament dynamics.
  • Generated deletions in myosin II components to assess motor activity effects.
  • Developed and simulated a quantitative microscopic model of actomyosin ring constriction.

Main Results:

  • Actin filament depolymerization significantly contributes to actomyosin ring constriction.
  • Disrupting depolymerization or myosin II function attenuated ring constriction.
  • Model simulations supported actin depolymerization as the predominant constriction mechanism.
  • Model predicted and experimental data confirmed that total contraction time is independent of initial ring size.

Conclusions:

  • Actin depolymerization is a primary driver of actomyosin ring constriction in budding yeast.
  • The interplay between actin dynamics and myosin II activity governs cell division timing.
  • The findings provide a mechanistic model for cytokinesis applicable across different cell sizes.