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

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

4.6K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
4.6K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

9.6K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
9.6K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

16.6K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
16.6K
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

4.5K
The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
4.5K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.6K
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...
2.6K
pH Regulation in Cells01:28

pH Regulation in Cells

7.5K
pH plays a critical role in maintaining normal cellular activities. It helps maintain the structure and function of various proteins, dictates the charge on cellular membranes, and is crucial for metabolic reactions inside the cell. Moreover, cells use the energy from the proton motive force to generate ATP.
Cytosolic pH
Under physiological conditions, the cytosolic pH is slightly more acidic than the extracellular pH. However, cells must prevent further acidification of their cytosol to...
7.5K

You might also read

Related Articles

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

Sort by
Same author

Spalt-related is an inhibitor of mTORC1-mediated growth activated by the integrated stress response.

The EMBO journal·2026
Same author

Towards the construction of a virtual yeast.

Nature·2026
Same author

MultiMS2: A curated multi-modal, multi-energy spectral library for metabolomics.

GigaScience·2026
Same author

eMZed 3: flexible and interactive development of scalable LC-MS/MS data analysis workflows in python.

Bioinformatics advances·2026
Same author

Excess glucose shapes mitochondrial metabolism and redox state in human primary white adipocytes.

Free radical biology & medicine·2026
Same author

Progressive Visual Recovery in a Patient with Leber Hereditary Optic Neuropathy Harboring a Rare Heteroplasmic (MT-ND5):m.13042G>A, p(Ala236Thr) Variant with Low Mutant Load: A Case Report.

Case reports in ophthalmology·2026

Related Experiment Video

Updated: Jan 9, 2026

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

2.2K

Vacuolar-type H+-ATPase-mediated extra-organellar buffering resolves mitochondrial dysfunction.

Geoffray Monteuuis1, Ryan Awadhpersad1, Daan van der Kolk1

  • 1Department of Biochemistry and Developmental Biology, Faculty of Medicine, University of Helsinki, Helsinki, Finland.

Nature Communications
|December 3, 2025
PubMed
Summary

Loss of vacuolar-type H+-ATPase (v-ATPase) surprisingly supports cell survival despite mitochondrial defects. This finding reveals a novel protective mechanism involving pH regulation and metabolic adaptation for cellular homeostasis.

More Related Videos

Microfluidics-Assisted Selective Depolarization of Axonal Mitochondria
06:55

Microfluidics-Assisted Selective Depolarization of Axonal Mitochondria

Published on: August 4, 2022

2.1K
Mitochondrial Ca2+ Retention Capacity Assay and Ca2+-triggered Mitochondrial Swelling Assay
05:53

Mitochondrial Ca2+ Retention Capacity Assay and Ca2+-triggered Mitochondrial Swelling Assay

Published on: May 1, 2018

11.9K

Related Experiment Videos

Last Updated: Jan 9, 2026

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

2.2K
Microfluidics-Assisted Selective Depolarization of Axonal Mitochondria
06:55

Microfluidics-Assisted Selective Depolarization of Axonal Mitochondria

Published on: August 4, 2022

2.1K
Mitochondrial Ca2+ Retention Capacity Assay and Ca2+-triggered Mitochondrial Swelling Assay
05:53

Mitochondrial Ca2+ Retention Capacity Assay and Ca2+-triggered Mitochondrial Swelling Assay

Published on: May 1, 2018

11.9K

Area of Science:

  • Cell Biology
  • Biochemistry
  • Genetics

Background:

  • Mitochondrial dysfunction is implicated in numerous human diseases, including neurodegeneration, cancer, and aging.
  • Cellular homeostasis relies on coordinated nuclear and mitochondrial gene expression.
  • Adaptive mechanisms are crucial for survival under cellular stress.

Purpose of the Study:

  • To identify cellular pathways that promote survival during impaired mitochondrial protein synthesis.
  • To investigate the role of vacuolar-type H+-ATPase (v-ATPase) in mitigating mitochondrial dysfunction.

Main Methods:

  • Genome-wide CRISPR knockout screening was employed to identify cell fitness pathways.
  • Experiments utilized cancer cell lines and patient-derived models of mitochondrial disease.

Main Results:

  • Loss of v-ATPase was identified as a potent suppressor of mitochondrial translation defects.
  • Partial v-ATPase loss modulated mitochondrial membrane potential (ΔΨm) and cristae structure.
  • This modulation occurred in both cancer cells and patient-derived mitochondrial disease models.

Conclusions:

  • v-ATPase acts as an extra-organellar buffering mechanism against mitochondrial dysfunction.
  • Altering pH homeostasis and metabolic rewiring are protective responses promoted by v-ATPase inhibition.
  • These adaptive strategies enhance cell fitness under conditions of mitochondrial stress.