Related Experiment Video
Updated: May 11, 2026
08:57
Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
Actin carbonylation: from cell dysfunction to organism disorder
José Pedro Castro1, Tobias Jung, Tilman Grune
1Departamento de Biologia Experimental, Faculdade de Medicina da Universidade do Porto, 4200-319 Porto, Portugal; IBMC-Instituto de Biologia Molecular e Celular, 4150-180 Porto, Portugal; Institute of Nutrition, Friedrich Schiller Universität Jena, Dornburger Str. 24, 07743 Jena, Germany.
Journal of Proteomics
|May 21, 2013
Summary
Protein carbonylation, a frequent and irreversible modification, damages proteins like actin, leading to aggregates and cell dysfunction. Insufficient protein repair mechanisms may drive aging and related diseases.
Area of Science:
- Biochemistry and Molecular Biology
- Cellular Biology
- Aging Research
Background:
- Protein carbonylation is a significant post-translational modification impacting proteostasis due to its irreversible nature.
- Carbonylated proteins can lead to dysfunction, aggregate formation, cellular senescence, and ultimately cell death.
- Actin, a crucial cytoskeletal protein, is highly susceptible to carbonylation.
Purpose of the Study:
- To review the susceptibility of actin to carbonylation under various conditions.
- To explore the cellular mechanisms involved in the removal of carbonylated actin.
- To discuss the implications of impaired protein repair in age-related diseases.
Main Methods:
- Literature review of studies investigating actin carbonylation.
- Analysis of data from cell-free extracts, cell lines, and animal models.
- Examination of cellular protein degradation pathways.
Main Results:
- Actin is frequently carbonylated, leading to loss of function and aggregation.
- Oxidative stress conditions exacerbate actin carbonylation.
- Cellular mechanisms for removing damaged proteins are often insufficient to cope with carbonylation burden.
Conclusions:
- Actin carbonylation contributes to cellular dysfunction and aggregate formation.
- The efficiency of protein repair pathways is critical in mitigating the effects of carbonylation.
- Impaired protein clearance mechanisms may play a role in aging and age-related pathologies.
More Related Videos
Related Concept Videos
01:13Actin 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.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.
01:42Actin 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...
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...
01:26Introduction to Actin
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.
01:19Actin 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...
In F-actin, the ADF/cofilin proteins...
01:30Carbohydrate Catabolism
Carbohydrate catabolism is a fundamental process in cellular metabolism that enables energy extraction from glucose through two primary pathways: cellular respiration and fermentation. Both pathways begin with glycolysis, which operates independently of oxygen availability.Glycolysis: A Shared Starting PointGlycolysis is an oxygen-independent process that breaks down glucose into two molecules of pyruvic acid. During this process, a net gain of two ATP molecules and two NADH molecules is...
01:19Overview of Carbohydrate Metabolism
Carbohydrate metabolism is a fundamental biochemical process that ensures a constant supply of energy to living cells. The most important carbohydrate is glucose, which can be broken down via glycolysis to enter into the Krebs cycle and eventually lead to the production of ATP through oxidative phosphorylation.
Glucose transport into cells is facilitated by a family of transport proteins called GLUT (Glucose Transporters). GLUT4 is the primary glucose transporter for insulin-stimulated glucose...
Glucose transport into cells is facilitated by a family of transport proteins called GLUT (Glucose Transporters). GLUT4 is the primary glucose transporter for insulin-stimulated glucose...