Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
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...
Peroxisomes01:30

Peroxisomes

Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.The peroxisome is a single membrane-bound cellular organelle that can perform several different functions, including lipid metabolism and chemical detoxification. The enzymes within peroxisomes...
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...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
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,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Modular Rh-Catalyzed Synthesis and Biological Profiling of Diverse Pentafluorobenzenesulfonamide Reactive Fragments.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Discovery of SHANK1-PDZ Peptide-Fragment Inhibitors Using a Dynamic Ligation Screening Strategy.

Biochemistry·2026
Same author

High-throughput discovery and characterisation of pentafluorobenzene sulfonamide modifiers of Aurora A kinase.

RSC chemical biology·2026
Same author

Predictive modelling of the COMATOSE transporter reveals a conserved ligand binding pocket for acyl-CoAs.

Scientific reports·2026
Same author

Covalent Peptide-Based N-Myc/Aurora-A Inhibitors Bearing Sulfonyl Fluoride Warheads.

Journal of peptide science : an official publication of the European Peptide Society·2026
Same author

Investigating the bioorthogonality of isocyanides.

Chemical communications (Cambridge, England)·2025
Same journal

TDP-43 proteinopathy as a biomarker and therapeutic target in amyotrophic lateral sclerosis.

Biochemical Society transactions·2026
Same journal

Advancing the monitoring of organelle contact sites in vitro and in vivo.

Biochemical Society transactions·2026
Same journal

Mechanisms influencing transient cytoplasmic protein targeting to intracellular lipid droplets.

Biochemical Society transactions·2026
Same journal

Replication associated nuclear DNA mismatch repair across kingdoms.

Biochemical Society transactions·2026
Same journal

Phosphatases of regenerating liver downregulate PTEN to promote tumorigenesis.

Biochemical Society transactions·2026
Same journal

Implications of Rho GTPase signaling in cancer immunotherapy.

Biochemical Society transactions·2026
See all related articles

Related Experiment Video

Updated: Jun 12, 2026

Monitoring Stub1-Mediated Pexophagy
08:26

Monitoring Stub1-Mediated Pexophagy

Published on: May 12, 2023

Peroxisome biogenesis and positioning.

Alison Baker1, Imogen A Sparkes, Laura-Anne Brown

  • 1Centre for Plant Sciences, University of Leeds, Leeds LS2 9JT, UK. a.baker@leeds.ac.uk

Biochemical Society Transactions
|May 25, 2010
PubMed
Summary
This summary is machine-generated.

Plant peroxisomes are dynamic organelles crucial for plant life. Their matrix and membrane proteins are imported through distinct pathways, involving complex machinery and protein turnover mechanisms.

More Related Videos

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

Using Fluorescent Proteins to Monitor Glycosome Dynamics in the African Trypanosome
10:04

Using Fluorescent Proteins to Monitor Glycosome Dynamics in the African Trypanosome

Published on: August 19, 2014

Related Experiment Videos

Last Updated: Jun 12, 2026

Monitoring Stub1-Mediated Pexophagy
08:26

Monitoring Stub1-Mediated Pexophagy

Published on: May 12, 2023

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

Using Fluorescent Proteins to Monitor Glycosome Dynamics in the African Trypanosome
10:04

Using Fluorescent Proteins to Monitor Glycosome Dynamics in the African Trypanosome

Published on: August 19, 2014

Area of Science:

  • Plant cell biology
  • Organelle biogenesis
  • Protein trafficking

Background:

  • Plant peroxisomes are highly dynamic organelles responding to environmental and metabolic cues.
  • Peroxisome matrix proteins are imported via two distinct pathways, each with specific receptors and shared translocation machinery.
  • Peroxisome membrane proteins utilize separate import mechanisms, potentially involving the endoplasmic reticulum.

Purpose of the Study:

  • To elucidate the mechanisms governing protein import into plant peroxisomes.
  • To explore the dynamics of peroxisome matrix and membrane protein trafficking.
  • To understand the role of protein import/turnover machinery in peroxisome function and biogenesis.

Main Methods:

  • Analysis of protein import pathways for peroxisome matrix proteins.
  • Investigation of receptor recycling and ubiquitination in import processes.
  • Characterization of machinery for peroxisome membrane protein targeting.
  • Utilizing mutants defective in peroxisome biogenesis for functional studies.

Main Results:

  • Identified two distinct import pathways for matrix proteins, each with unique receptors but common translocation components.
  • Proposed receptor recycling mechanisms potentially involving ubiquitination cycles.
  • Highlighted parallels between peroxisomal protein import/turnover and endoplasmic-reticulum-associated degradation.
  • Demonstrated distinct machinery for peroxisome membrane protein import, including post-translational and ER-trafficked routes.
  • Emphasized the essential role of peroxisomes throughout the plant life cycle via mutant studies.

Conclusions:

  • Plant peroxisome protein import is a complex, multi-pathed process crucial for organelle function.
  • Protein turnover and import machinery share components and mechanisms, highlighting cellular coordination.
  • Peroxisome biogenesis and function are vital at all stages of plant development.