Related Experiment Video
Updated: May 4, 2026

08:26
Monitoring Stub1-Mediated Pexophagy
Published on: May 12, 2023
2.3K
The peroxisomal receptor dislocation pathway: to the exportomer and beyond.
Harald W Platta1, Stefanie Hagen2, Christina Reidick1
1Biochemie Intrazellulärer Transportprozesse, Ruhr-Universität Bochum, Universitätsstr. 150, D-44780 Bochum, Germany.
Biochimie
|December 19, 2013
Summary
The peroxisomal exportomer machinery facilitates matrix protein import via ubiquitination and extraction. This system also plays roles in plant photorespiration, fungal development, and peroxisome degradation.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Peroxisome biogenesis relies on ubiquitin-dependent import of matrix proteins.
- Import receptors bind matrix proteins via peroxisomal targeting sequences (PTS) and are recycled.
- The exportomer machinery mediates receptor extraction from the peroxisomal membrane.
Purpose of the Study:
- To review the central role of the peroxisomal exportomer in matrix protein import.
- To highlight distinct cellular functions of exportomer components beyond receptor recycling.
Main Methods:
- Literature review of existing research on peroxisome biogenesis and exportomer function.
- Analysis of studies investigating the mechanistic links between protein translocation and receptor extraction.
- Synthesis of evidence for diverse roles of exportomer components in plants and fungi.
Main Results:
- The exportomer utilizes ubiquitination and ATP-dependent extraction for PTS-receptor retrotranslocation.
- Evidence suggests interconnectedness between matrix protein translocation and receptor removal.
- Exportomer components are implicated in plant photorespiration, fungal meiocyte formation, and pexophagy.
Conclusions:
- The peroxisomal exportomer is crucial for matrix protein import and receptor recycling.
- Exportomer constituents have diverse, non-canonical functions in various cellular processes.
- Further research is needed to fully elucidate the multifaceted roles of the exportomer.
Related Concept Videos
Protein Import into the Peroxisomes
4.4K
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...
4.4K
Peroxisomes
13.6K
Peroxisomes are specialized organelles present in fungi, plant, and animal cells. It can vary in number, size, morphology, and activity depending on the type of tissue and the nutritional state of the cell. For example, cells with active lipid metabolism, such as adipocytes, neurons, and hepatocytes, have more peroxisomes than other cells in the body. Besides their primary role in breaking down complex organic molecules, peroxisomes can also synthesize specific macromolecules and participate in...
13.6K
Peroxisomes
1.8K
1.8K
Export of Misfolded Proteins out of the ER
4.3K
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...
4.3K
Nuclear Export
3.7K
The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
3.7K
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

