Related Experiment Video
Updated: Jun 26, 2025

08:26
Monitoring Stub1-Mediated Pexophagy
Published on: May 12, 2023
1.6K
Mammalian pexophagy at a glance.
Justyna Bajdzienko1, Anja Bremm1
1Goethe University Frankfurt, Medical Faculty , Institute of Biochemistry II, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany.
Journal of Cell Science
|May 16, 2024
Summary
Mammalian pexophagy, the process of removing damaged peroxisomes, is crucial for cell health. This review highlights ubiquitylation
Area of Science:
- Cell Biology
- Organelle Biology
- Autophagy
Background:
- Peroxisomes are vital organelles regulating metabolism and redox balance.
- Their numbers dynamically adjust to nutrient and stress conditions.
- Pexophagy, or selective peroxisome autophagy, removes damaged or excess peroxisomes.
Purpose of the Study:
- To summarize current knowledge on mammalian pexophagy control.
- To identify areas needing further research in mammalian pexophagy.
- To discuss the role of ubiquitylation in pexophagy.
Main Methods:
- Review of current literature on mammalian pexophagy.
- Analysis of ubiquitylation pathways in pexophagy.
- Comparison of mammalian and yeast pexophagy mechanisms.
Main Results:
- Mammalian pexophagy is induced by ubiquitylation of peroxisomal proteins or ubiquitin-independent pathways.
- Dysregulation of pexophagy is linked to human diseases.
- Ubiquitin machinery plays a key role in recruiting phagophores to peroxisomes.
Conclusions:
- Understanding mammalian pexophagy is crucial for maintaining peroxisome homeostasis.
- Further research is needed to fully elucidate mammalian pexophagy mechanisms.
- Ubiquitylation is a central regulator of pexophagy.
More Related Videos
Related Concept Videos
Phagocytosis
80.0K
Cells pull particles inward and engulf them in spherical vesicles in an energy-requiring process called endocytosis. Phagocytosis (“cellular eating”) is one of three major types of endocytosis. Cells use phagocytosis to take in large objects—such as other cells (or their debris), bacteria, and even viruses.
80.0K
Protein Import into the Peroxisomes
3.5K
Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
3.5K
Delivery Pathways to the Lysosome
6.3K
Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
6.3K
Autophagy
4.2K
Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
4.2K
The Proteasome Structure
747
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The proteasome is an...
747
Export of Misfolded Proteins out of the ER
3.6K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
3.6K

