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

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

9.8K
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,...
9.8K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

5.1K
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...
5.1K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.4K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.4K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.7K
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...
2.7K
Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

971
The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...
971
Mitochondrial Membranes01:45

Mitochondrial Membranes

14.6K
A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
14.6K

You might also read

Related Articles

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

Sort by
Same author

Commentary: Why do many cell biology papers contain fundamental bioenergetic errors?

Biochimica et biophysica acta. Bioenergetics·2025
Same author

Does a transmembrane sodium gradient control membrane potential in mammalian mitochondria?

Cell calcium·2024
Same author

Global assessment of marine plastic exposure risk for oceanic birds.

Nature communications·2023
Same author

Fifty years on: How we uncovered the unique bioenergetics of brown adipose tissue.

Acta physiologica (Oxford, England)·2023
Same author

A critical assessment of the role of creatine in brown adipose tissue thermogenesis.

Nature metabolism·2023
Same author

Solid Phase Synthesis of Dual Labeled Peptides: Development of Cell Permeable Calpain Specific Substrates.

International journal of peptide research and therapeutics·2020

Related Experiment Video

Updated: Nov 10, 2025

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
07:35

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

Published on: June 1, 2022

2.4K

Mitochondrial proton leaks and uncoupling proteins.

David G Nicholls1

  • 1Buck Institute for Research on Aging, Novato, CA, USA.

Biochimica Et Biophysica Acta. Bioenergetics
|April 2, 2021
PubMed
Summary
This summary is machine-generated.

Brown adipose tissue thermogenesis relies on uncoupling protein 1 (UCP1). This review critically examines UCP1 regulation mechanisms and discusses UCP1-independent proton leak and related proteins.

Keywords:
Brown adipose tissueBrown fatMitochondriaUCP1UCP2UCP3Uncoupling protein

More Related Videos

The Use of the Patch-Clamp Technique to Study the Thermogenic Capacity of Mitochondria
11:05

The Use of the Patch-Clamp Technique to Study the Thermogenic Capacity of Mitochondria

Published on: May 3, 2021

4.1K
Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

2.1K

Related Experiment Videos

Last Updated: Nov 10, 2025

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
07:35

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

Published on: June 1, 2022

2.4K
The Use of the Patch-Clamp Technique to Study the Thermogenic Capacity of Mitochondria
11:05

The Use of the Patch-Clamp Technique to Study the Thermogenic Capacity of Mitochondria

Published on: May 3, 2021

4.1K
Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

2.1K

Area of Science:

  • Mitochondrial physiology
  • Cellular metabolism
  • Thermogenesis

Background:

  • Non-shivering thermogenesis is primarily mediated by uncoupling protein 1 (UCP1) in brown adipose tissue.
  • UCP1 facilitates proton re-entry into the mitochondrial inner membrane, uncoupling respiration from ATP synthesis.
  • Decades of research have yielded extensive, yet often contradictory, findings on UCP1 regulation.

Purpose of the Study:

  • To critically review the experimental evidence for proposed UCP1 regulatory mechanisms.
  • To evaluate the methodologies used in UCP1 research in relation to physiological context.
  • To discuss UCP1-independent proton leak and the roles of UCP2 and UCP3.

Main Methods:

  • Comprehensive literature review of studies on UCP1.
  • Analysis of experimental methodologies and their physiological relevance.
  • Evaluation of evidence for fatty acid, purine nucleotide, and other regulatory factors.

Main Results:

  • The physiological regulation of UCP1 by fatty acids and nucleotides is complex and debated.
  • Methodological limitations have contributed to conflicting findings in the field.
  • Endogenous proton leak pathways independent of UCP1 exist.

Conclusions:

  • A thorough re-evaluation of UCP1 regulation is needed, considering cellular context.
  • The roles and regulation of UCP2 and UCP3 remain unclear and require further investigation.
  • Understanding UCP1 function is crucial for metabolic and thermogenic research.