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Related Concept Videos

Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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,...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Peroxisomes01:24

Peroxisomes

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...

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Related Experiment Video

Updated: Jul 15, 2026

Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes
05:57

Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes

Published on: December 19, 2025

The peroxisomal protein import machinery.

Harald W Platta1, Ralf Erdmann

  • 1Abteilung für Systembiochemie, Medizinische Fakultät der Ruhr-Universität Bochum, D-44780 Bochum, Germany.

FEBS Letters
|April 21, 2007
PubMed
Summary

Peroxisomes dynamically regulate their protein content via import machineries involving at least 20 peroxins. Receptor recycling, crucial for matrix protein import, requires ATP for ubiquitination and dislocation.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Peroxisomes are vital organelles with adaptable functions influenced by cellular context and organismal state.
  • Their dynamic enzyme content relies on sophisticated protein import systems involving numerous peroxins (peroxisomal biogenesis factors).

Purpose of the Study:

  • To elucidate the molecular mechanisms governing peroxisomal matrix protein import.
  • To understand the role of cycling receptors and the energy-dependent steps in protein translocation.

Main Methods:

  • The study focuses on the import machinery of peroxisomal matrix proteins.
  • Investigates the function of cycling receptors mediating protein transport between the cytosol and peroxisomal lumen.

Main Results:

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Monitoring Stub1-Mediated Pexophagy

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Peroxisome Staining in Mammalian Cells Using Peroxisome-Specific Probes
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  • Peroxisomal matrix protein import is mediated by cycling receptors that shuttle between cellular compartments.
  • Receptor release back into the cytosol is an ATP-dependent process.
  • This energy-dependent step involves receptor ubiquitination and subsequent dislocation.

Conclusions:

  • The import of folded peroxisomal matrix proteins relies on a complex, receptor-mediated system.
  • Energy, in the form of ATP, is essential for the final stages of receptor recycling, highlighting key regulatory steps in peroxisome biogenesis.