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

The Electron Transport Chain01:30

The Electron Transport Chain

17.3K
The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
17.3K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.6K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
2.6K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

15.0K
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
15.0K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.2K
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,...
3.2K
Pyruvate Oxidation01:15

Pyruvate Oxidation

161.0K
After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
161.0K
Electron Transport Chains01:28

Electron Transport Chains

102.4K
The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...
102.4K

You might also read

Related Articles

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

Sort by
Same author

A clinical study examining the effects of dietary nitrate on urinary N-nitrosamines.

The American journal of clinical nutrition·2026
Same author

Sera from patients with dermatomyositis and antisynthetase syndrome mediate muscle weakness, impair mitochondrial respiration and induce local cytokine production in muscle tissue.

Journal of autoimmunity·2026
Same author

Exploratory study linking plasma proteomics to cardiotoxicity in Hodgkin lymphoma.

Cardio-oncology (London, England)·2025
Same author

The sodium/iodide symporter is a nitrate transporter in the human salivary gland.

Redox biology·2025
Same author

The ghrelin receptor agonist AC01 improves cardiomyocyte contractility through Gαi signalling and without Ca2+ mobilization.

Cardiovascular research·2025
Same author

Dietary Nitrate Prevents Cardiac Dysfunction in HFrEF by Improving Hemodynamics, Ameliorating Remodeling, and Resolving Inflammation.

Acta physiologica (Oxford, England)·2025

Related Experiment Video

Updated: Sep 8, 2025

Mitochondrial Respiration Quantification in Yeast Whole Cells
07:15

Mitochondrial Respiration Quantification in Yeast Whole Cells

Published on: November 8, 2024

696

Mitochondrial Respiration-Dependent ANT2-UCP2 Interaction.

Tomas A Schiffer1, Liza Löf2, Radiosa Gallini2

  • 1Department of Physiology and Pharmacology, Karolinska Institutet, Solna, Sweden.

Frontiers in Physiology
|June 13, 2022
PubMed
Summary

Adenine nucleotide translocases (ANTs) and uncoupling proteins (UCPs) interact, with their association regulated by cellular metabolism. This interaction influences mitochondrial proton leak and may affect cellular substrate utilization.

Keywords:
adenine nucleotide translocase-2mitochondriaprotein interactionproximity ligation assayuncoupling protein-2

More Related Videos

Using Isolated Mitochondria from Minimal Quantities of Mouse Skeletal Muscle for High throughput Microplate Respiratory Measurements
10:39

Using Isolated Mitochondria from Minimal Quantities of Mouse Skeletal Muscle for High throughput Microplate Respiratory Measurements

Published on: October 30, 2015

13.9K
Isolation of Mitochondria from Mouse Skeletal Muscle for Respirometric Assays
08:11

Isolation of Mitochondria from Mouse Skeletal Muscle for Respirometric Assays

Published on: February 10, 2022

5.3K

Related Experiment Videos

Last Updated: Sep 8, 2025

Mitochondrial Respiration Quantification in Yeast Whole Cells
07:15

Mitochondrial Respiration Quantification in Yeast Whole Cells

Published on: November 8, 2024

696
Using Isolated Mitochondria from Minimal Quantities of Mouse Skeletal Muscle for High throughput Microplate Respiratory Measurements
10:39

Using Isolated Mitochondria from Minimal Quantities of Mouse Skeletal Muscle for High throughput Microplate Respiratory Measurements

Published on: October 30, 2015

13.9K
Isolation of Mitochondria from Mouse Skeletal Muscle for Respirometric Assays
08:11

Isolation of Mitochondria from Mouse Skeletal Muscle for Respirometric Assays

Published on: February 10, 2022

5.3K

Area of Science:

  • Mitochondrial physiology
  • Cellular metabolism
  • Protein-protein interactions

Background:

  • Adenine nucleotide translocases (ANTs) and uncoupling proteins (UCPs) are involved in mitochondrial proton leak.
  • Previous studies suggest UCP2/3 knockdown increases ANT-dependent proton leak.
  • UCP2 is implicated in C4 metabolite efflux from the mitochondrial matrix.

Purpose of the Study:

  • To investigate the interaction between UCP2 and ANT2 proteins.
  • To determine if this interaction is regulated by cellular metabolic demand.
  • To elucidate the role of ANT2-UCP2 interaction in mitochondrial proton leak.

Main Methods:

  • Reciprocal co-immunoprecipitation and in situ proximity ligation assays to assess protein-protein interaction.
  • siRNA-mediated knockdown of ANT2 and UCP2 in HEK293A cells.
  • High-resolution respirometry to measure mitochondrial and cellular respiration.

Main Results:

  • Demonstrated a direct interaction between ANT2 and UCP2, dependent on cellular metabolism.
  • Inhibition of ATP synthase promoted ANT2-UCP2 interaction; FCCP-induced respiration prevented it.
  • UCP2 knockdown increased proton leak, but double knockdown of ANT2 and UCP2 reduced it compared to UCP2 knockdown alone.

Conclusions:

  • ANT2 and UCP2 interact dynamically, regulated by mitochondrial respiratory activity.
  • This interaction may play a role in regulating mitochondrial efficiency.
  • UCP2 activity could influence the switch between glucose and fatty acid metabolism.