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Published on: July 30, 2014
A role for actin in aging and apoptosis
1Department of Molecular Biology and Biotechnology, Firth Court, University of Sheffield, Western Bank, Sheffield S10 2TN, UK.
Biochemical Society Transactions
|October 26, 2005
Summary
Actin dynamics influence cell death and longevity in yeast. Increased actin dynamics promote survival by reducing reactive oxygen species (ROS), while decreased dynamics increase ROS and decrease viability.
Area of Science:
- Cell Biology
- Aging Research
- Biochemistry
Background:
- The actin cytoskeleton is crucial for fundamental cellular processes like membrane trafficking and polarity.
- Cellular aging in Saccharomyces cerevisiae (yeast) resembles an apoptotic-like pathway.
- This pathway involves DNA fragmentation, mitochondrial dysfunction, increased reactive oxygen species (ROS), and phosphatidylserine exposure.
Purpose of the Study:
- To investigate the role of the actin cytoskeleton in yeast cell death and longevity.
- To understand how alterations in actin dynamics affect aging and survival pathways.
Main Methods:
- Utilizing Saccharomyces cerevisiae as a model organism.
- Monitoring actin dynamics and correlating them with cellular aging markers.
- Measuring reactive oxygen species (ROS) levels and cell viability.
Main Results:
- Reduced actin dynamics correlate with elevated ROS levels and diminished cell viability.
- Increased actin dynamics are associated with lower ROS levels and enhanced cell survival.
- Alterations in actin dynamics can trigger the apoptotic-like cell death pathway.
Conclusions:
- Actin dynamics play a significant role in regulating cell death and promoting longevity in yeast.
- Modulating actin dynamics offers a potential strategy for influencing cellular aging.
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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 different species.
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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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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).
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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.
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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.

