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Related Concept Videos

Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

5.6K
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...
5.6K
Peroxisomes01:24

Peroxisomes

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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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Peroxisomes01:24

Peroxisomes

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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

5.1K
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

5.9K
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...
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Monitoring Stub1-Mediated Pexophagy
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Peroxisome protein import: a complex journey.

Alison Baker1, Thomas Lanyon-Hogg2, Stuart L Warriner3

  • 1School of Molecular and Cellular Biology, Astbury Centre for Structural Molecular Biology and Centre for Plant Sciences, University of Leeds, Leeds LS2 9JT, U.K. a.baker@leeds.ac.uk.

Biochemical Society Transactions
|June 11, 2016
PubMed
Summary

Protein import into peroxisomes is complex, involving folded proteins and diverse signals. Recent studies reveal intricate cargo-receptor interactions and conformational changes in the PEX5 receptor crucial for import and recycling.

Keywords:
PEX5mechanismsmodelsperoxisomeprotein import cycletargeting signal

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Peroxisomal protein import is essential for cellular function.
  • It exhibits unique characteristics, including the import of folded proteins and varied targeting signals.
  • The protein import machinery involves a complex network of factors.

Purpose of the Study:

  • To provide an update on recent literature regarding protein import mechanisms into peroxisomes.
  • To highlight the complexity of the peroxisomal protein import pathway.
  • To discuss recent findings on receptor-cargo interactions and conformational changes.

Main Methods:

  • Review of recent scientific literature.
  • Analysis of structural studies on protein-receptor interactions.
  • Examination of biochemical data on import and recycling mechanisms.

Main Results:

  • Protein import into peroxisomes involves folded proteins and diverse targeting signals.
  • Structural studies reveal cargo-induced conformational changes in the PEX5 receptor.
  • Biochemical studies show interdependence between receptor-cargo import and receptor release.

Conclusions:

  • The peroxisomal protein import pathway is intricate, with complex interactions between cargo and receptors.
  • Conformational changes in the PEX5 receptor are critical for the import process.
  • Efficient import and recycling of the PEX5 receptor are interdependent.