Related Experiment Video
Updated: May 5, 2026

07:56
Visualizing Mitophagy with Fluorescent Dyes for Mitochondria and Lysosome
Published on: November 30, 2022
6.0K
Aging: filtering out bad mitochondria
1Department of Chemistry and Molecular Biology, University of Gothenburg, Medicinaregatan 9C, S-413 90 Göteborg, Sweden.
Current Biology : CB
|December 7, 2013
Summary
Yeast cells rejuvenate during division by filtering out old, damaged mitochondria. This process relies on Sir2 and actin cables, ensuring daughter cells receive healthy mitochondria.
Area of Science:
- Cell biology
- Molecular biology
- Genetics
Background:
- Cellular aging and rejuvenation are critical biological processes.
- Cytokinesis, the process of cell division, requires precise partitioning of cellular components.
- Mitochondrial quality control is essential for maintaining cellular health.
Purpose of the Study:
- To investigate the mechanisms underlying rejuvenation during yeast cytokinesis.
- To identify factors involved in the selective inheritance of mitochondria.
- To understand how cellular aging is reversed in daughter cells.
Main Methods:
- Yeast genetics and live-cell imaging were employed.
- Sir2 (Silent information regulator 2) protein localization was tracked.
- Actin cable dynamics during cytokinesis were analyzed.
- Mitochondrial morphology and function were assessed in mother and daughter cells.
Main Results:
- A novel filtering mechanism was identified during yeast cytokinesis.
- This process depends on the Sir2 protein and actin cables.
- Feeble mitochondria were actively prevented from entering the daughter cell.
- Daughter cells inherited primarily healthy mitochondria, indicating rejuvenation.
Conclusions:
- Yeast cytokinesis involves a Sir2- and actin-cable-dependent process to ensure daughter cell rejuvenation.
- This mechanism selectively removes aged or damaged mitochondria.
- The findings provide new insights into asymmetric cell division and aging.
Related Concept Videos
Electron Transport Chain: Complex I and II
11.9K
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
ROS generation is regulated and maintained at moderate levels necessary...
11.9K
Mitochondria
13.4K
Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
13.4K
Mitochondrial Membranes
11.7K
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
11.7K
Translocation of Proteins into the Mitochondria
8.8K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
8.8K

