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

Energy to Drive Translocation01:37

Energy to Drive Translocation

2.9K
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...
2.9K
Mitochondrial Membranes01:45

Mitochondrial Membranes

17.6K
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,...
17.6K
Mitochondrial Membranes01:45

Mitochondrial Membranes

2.2K
2.2K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

13.6K
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,...
13.6K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

3.9K
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...
3.9K
Chemiosmosis01:32

Chemiosmosis

116.3K
Oxidative phosphorylation is a highly efficient process that generates large amounts of adenosine triphosphate (ATP), the basic unit of energy that drives many cellular processes. Oxidative phosphorylation involves two processes— the electron transport chain and chemiosmosis.
Electron Transport Chain
The electron transport chain involves a series of protein complexes on the inner mitochondrial membrane that undergo a series of redox reactions. At the end of this chain, the electrons...
116.3K

You might also read

Related Articles

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

Sort by
Same author

Distinct hydrolyzed Al-Ti species govern the coagulation behavior and subsequent anaerobic fermentation of CEPS sludge.

Water research·2026
Same author

The anion channel SLAH3 regulates flowering time in Arabidopsis thaliana.

Biochemical and biophysical research communications·2026
Same author

A bulk cell heterozygous knock-in strategy for targeted protein degradation.

bioRxiv : the preprint server for biology·2026
Same author

Development and Validation of a Nomogram for Predicting Sepsis Risk in Patients with Non-Ventilator Hospital-Acquired Pneumonia.

Biomedicines·2026
Same author

Dual-functional chitosan-hyaluronic acid dialdehyde nanoparticles for CD44-targeted Bcl-2 siRNA delivery and photothermal therapy in bladder cancer.

Journal of biotechnology·2026
Same author

Identification of Potential Oxidative Stress-Related Causal Genes for Calculus of Kidney and Ureter: A Multi-Omics Mendelian Randomization Analysis.

Kidney diseases (Basel, Switzerland)·2026
Same journal

Enhanced-Sampling Simulations Reveal Distinct Intermediates in SARS-CoV-2 FSE Pseudoknot Interconversion.

Biophysical journal·2026
Same journal

Structure-based simulations of the full Flock House virus capsid reveal pathways and energetics of an infection-critical peptide externalization event.

Biophysical journal·2026
Same journal

Quantifying the Peripheral Surface Information Entropy from Conformational Ensembles of Globular Protein-Peptide Complexes.

Biophysical journal·2026
Same journal

Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

Biophysical journal·2026
Same journal

Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.

Biophysical journal·2026
Same journal

Dynamic conformations of fluorophores on self-labeling protein tags.

Biophysical journal·2026
See all related articles

Related Experiment Video

Updated: Mar 17, 2026

Photostimulation by Femtosecond Laser Activates Extracellular-signal-regulated Kinase ERK Signaling or Mitochondrial Events in Target Cells
11:00

Photostimulation by Femtosecond Laser Activates Extracellular-signal-regulated Kinase ERK Signaling or Mitochondrial Events in Target Cells

Published on: July 6, 2019

7.3K

Protons Trigger Mitochondrial Flashes.

Xianhua Wang1, Xing Zhang2, Zhanglong Huang1

  • 1State Key Laboratory of Membrane Biology, Peking-Tsinghua Center for Life Sciences, Institute of Molecular Medicine, Peking University, Beijing, China.

Biophysical Journal
|July 28, 2016
PubMed
Summary
This summary is machine-generated.

Mitochondrial flashes (mitoflashes) are triggered by nanodomain protons within mitochondria. This discovery reveals a novel link between proton signaling and mitochondrial energy metabolism.

More Related Videos

Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo
12:06

Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo

Published on: November 5, 2013

15.2K
Assessment of Mitochondrial Fission/Fusion Dynamics in Kidney Proximal Tubular Cells
06:14

Assessment of Mitochondrial Fission/Fusion Dynamics in Kidney Proximal Tubular Cells

Published on: November 14, 2025

701

Related Experiment Videos

Last Updated: Mar 17, 2026

Photostimulation by Femtosecond Laser Activates Extracellular-signal-regulated Kinase ERK Signaling or Mitochondrial Events in Target Cells
11:00

Photostimulation by Femtosecond Laser Activates Extracellular-signal-regulated Kinase ERK Signaling or Mitochondrial Events in Target Cells

Published on: July 6, 2019

7.3K
Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo
12:06

Confocal Imaging of Single Mitochondrial Superoxide Flashes in Intact Heart or In Vivo

Published on: November 5, 2013

15.2K
Assessment of Mitochondrial Fission/Fusion Dynamics in Kidney Proximal Tubular Cells
06:14

Assessment of Mitochondrial Fission/Fusion Dynamics in Kidney Proximal Tubular Cells

Published on: November 14, 2025

701

Area of Science:

  • Mitochondrial physiology
  • Cellular signaling
  • Bioenergetics

Background:

  • Mitochondrial flashes (mitoflashes) are conserved signaling events.
  • The precise triggers and integration of mitoflashes with mitochondrial functions are not fully understood.

Purpose of the Study:

  • To identify the specific signal components that initiate mitoflashes.
  • To elucidate the trigger mechanism underlying mitoflash generation.

Main Methods:

  • Utilized multiple biosensors and chemical probes.
  • Employed label-free autofluorescence techniques.
  • Performed numerical simulations for proton dynamics.

Main Results:

  • Mitoflashes involve superoxide bursts, redox shifts, matrix alkalinization, and membrane depolarization.
  • Electroneutral proton transport and matrix proton uncaging triggered mitoflashes.
  • Charge-uncompensated proton transport and acidification inhibited mitoflashes.
  • Estimated proton lifetime (1.42 ns) and diffusion distance (2.06 nm) in the mitochondrial matrix.

Conclusions:

  • Nanodomain protons serve as a novel trigger for mitoflashes in energized mitochondria.
  • Mitoflash genesis is mechanistically and functionally linked to mitochondrial energy metabolism.