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Related Concept Videos

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 Polymerization01:42

Actin Polymerization

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 actin...
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.
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

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 networks...
Actin Treadmilling01:18

Actin Treadmilling

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...
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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Reconstitution of Actin-Based Motility with Commercially Available Proteins
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Reconstitution of Actin-Based Motility with Commercially Available Proteins

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Cortical actin dynamics: Generating randomness by formin(g) and moving.

Haochen Yu1, Roland Wedlich-Söldner

  • 1Institute of Biochemistry; ETH Zürich; Zurich, Switzerland.

Bioarchitecture
|November 10, 2011
PubMed
Summary
This summary is machine-generated.

Budding yeast actin cables are surprisingly dynamic in G1 cells, driven by formin Bni1 and Myosin V. This study reveals a novel mechanism for cellular organization through regulated actin cable dynamics.

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Area of Science:

  • Cell Biology
  • Cytoskeleton Dynamics
  • Budding Yeast Model System (Saccharomyces cerevisiae)

Background:

  • The actin cytoskeleton is crucial for cell polarization and morphogenesis in Saccharomyces cerevisiae.
  • Formin-generated actin cables serve as tracks for polarized transport, driving Cdc42-dependent cell polarization.
  • Previous research primarily focused on static actin cables in polarized budded cells.

Purpose of the Study:

  • To characterize the dynamics of cortical actin cables throughout the entire yeast cell cycle.
  • To investigate the molecular mechanisms regulating actin cable dynamics and organization.
  • To understand the role of actin cable dynamics in cellular organization.

Main Methods:

  • Quantitative live-cell imaging of actin cable dynamics.
  • Analysis of actin cable behavior across different cell cycle stages.
  • Investigating the roles of specific proteins like formins and myosins.

Main Results:

  • Cortical actin cables in G1 phase yeast cells exhibit the highest level of dynamic behavior.
  • Actin cable dynamics significantly decrease upon cell polarization.
  • Rapid dynamics of randomly oriented cables are mediated by the formin Bni1 and Myosin V.
  • Evidence for myosin-mediated actin cable rearrangement.

Conclusions:

  • Actin cable dynamics are precisely regulated in a spatio-temporal manner throughout the yeast cell cycle.
  • Myosins play an unexpected role in the rearrangement of actin cables.
  • Generating randomness in actin cable dynamics is essential for cellular organization and polarization.