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Related Concept Videos

Protein Import into the Peroxisomes01:27

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...
3.5K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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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,...
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

3.7K
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...
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

4.3K
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...
4.3K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.6K
Peroxisomes01:24

Peroxisomes

12.2K
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: Jun 28, 2025

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria
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ATP-Dependent Steps in Peroxisomal Protein Import.

Harald W Platta1, Julia Jeske2, Nadine Schmidt2

  • 1Biochemie Intrazellulärer Transportprozesse, Ruhr-Universität Bochum, Bochum, Germany;

Annual Review of Biochemistry
|April 15, 2024
PubMed
Summary

Peroxisome protein import relies on ATP-dependent receptor recycling. Monoubiquitination and AAA+ peroxins drive the release of receptors, enabling further cargo import.

Keywords:
AAA+ peroxinsimport receptorperoxisomesprotein quality controlprotein transportubiquitination

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Area of Science:

  • Cell Biology
  • Molecular Biology

Background:

  • Peroxisomes are vital organelles involved in lipid metabolism and redox balance.
  • Protein import into peroxisomes requires specific targeting signals and receptors.
  • The import process is known to be ATP-dependent, but the exact timing of energy utilization has been debated.

Purpose of the Study:

  • To elucidate the ATP-dependent steps in peroxisomal protein import.
  • To detail the role of receptor ubiquitination and AAA+ peroxins in this process.
  • To provide an overview of recent findings on peroxisome protein import mechanisms.

Main Methods:

  • Review of existing literature on peroxisome biogenesis and protein import.
  • Analysis of biochemical pathways involving peroxisomal targeting signal (PTS) receptors.
  • Discussion of the role of monoubiquitination and AAA+ peroxins in receptor recycling.

Main Results:

  • The ATP-dependent steps occur late in the import cycle, linked to receptor release.
  • Cysteine-dependent monoubiquitination of PTS receptors is crucial for their recognition by AAA+ peroxins.
  • AAA+ peroxins utilize ATP to extract ubiquitinated receptors from the membrane for cytosolic release.

Conclusions:

  • Peroxisome protein import is an energy-intensive process involving late-acting, ATP-dependent receptor recycling.
  • Ubiquitination and deubiquitination cycles regulate the competence of PTS receptors for cargo import.
  • Understanding these ATP-dependent steps is key to comprehending peroxisome function and biogenesis.