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

Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
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,...
Mitochondrial Membranes01:45

Mitochondrial Membranes

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,...
Mitochondrial Membranes01:45

Mitochondrial Membranes

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,...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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 precursors...
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

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...

You might also read

Related Articles

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

Sort by
Same author

Miniaturized optical system for a chip-based cold-atom inertial sensor.

Applied optics·2025
Same author

S1R agonist modulates rat platelet eicosanoid synthesis and aggregation.

Platelets·2021
Same author

Functionalization of gold nanoparticles with amino acid, beta-amyloid peptides and fragment.

Colloids and surfaces. B, Biointerfaces·2010
Same author

Transposon Tn917PF1 mutagenesis in Bacillus licheniformis.

Microbiology (Reading, England)·2009
Same author

Effects of sex hormones on ECG parameters and expression of cardiac ion channels in dogs.

Acta physiologica (Oxford, England)·2006
Same author

Evaluation of rat and rabbit sera lipoproteins in experimentally induced hyperlipidemia by analytical ultracentrifugation.

European biophysics journal : EBJ·2005

Related Experiment Video

Updated: Jun 28, 2026

High-Throughput Image-Based Quantification of Mitochondrial DNA Synthesis and Distribution
10:47

High-Throughput Image-Based Quantification of Mitochondrial DNA Synthesis and Distribution

Published on: May 5, 2023

When is high-Ca+ microdomain required for mitochondrial Ca+ uptake?

A Spät1, L Fülöp, P Koncz

  • 1Department of Physiology, Faculty of Medicine, Semmelweis University, Budapest, Hungary. spat@puskin.sote.hu

Acta Physiologica (Oxford, England)
|November 6, 2008
PubMed
Summary

High-calcium microdomains near the endoplasmic reticulum regulate mitochondrial calcium uptake. Protein kinase and phosphatase activity influences this process, protecting cells from overload and apoptosis.

More Related Videos

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

An In Vitro Approach to Study Mitochondrial Dysfunction: A Cybrid Model
06:05

An In Vitro Approach to Study Mitochondrial Dysfunction: A Cybrid Model

Published on: March 9, 2022

Related Experiment Videos

Last Updated: Jun 28, 2026

High-Throughput Image-Based Quantification of Mitochondrial DNA Synthesis and Distribution
10:47

High-Throughput Image-Based Quantification of Mitochondrial DNA Synthesis and Distribution

Published on: May 5, 2023

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

An In Vitro Approach to Study Mitochondrial Dysfunction: A Cybrid Model
06:05

An In Vitro Approach to Study Mitochondrial Dysfunction: A Cybrid Model

Published on: March 9, 2022

Area of Science:

  • Cell Biology
  • Mitochondrial Function
  • Calcium Signaling

Background:

  • Calcium (Ca2+) release from the endoplasmic reticulum (ER) creates localized high-Ca2+ microdomains.
  • These microdomains are situated between ER vesicles and neighboring mitochondria.
  • The role of these microdomains in mitochondrial Ca2+ uptake is not fully understood.

Purpose of the Study:

  • To model the conditions under which high-Ca2+ microdomains are necessary for mitochondrial Ca2+ uptake.
  • To investigate the influence of protein kinases and phosphatases on mitochondrial Ca2+ uptake.
  • To explain differential mitochondrial Ca2+ signaling responses.

Main Methods:

  • Utilized angiotensin II-stimulated H295R adrenocortical cells.
  • Manipulated p38 mitogen-activated protein kinase (MAPK) and protein kinase C (PKC) activity via silencing or inhibition.
  • Inhibited protein phosphatases to assess their impact on Ca2+ uptake.

Main Results:

  • Mitochondrial Ca2+ uptake correlated with ER-mitochondrion proximity in stimulated cells.
  • Inhibition of p38 MAPK or novel PKC isoforms enhanced mitochondrial Ca2+ uptake.
  • Protein phosphatase inhibition attenuated mitochondrial Ca2+ uptake.
  • These manipulations abolished the correlation between Ca2+ uptake and ER-mitochondrion proximity.

Conclusions:

  • High-Ca2+ microdomains are crucial for mitochondrial Ca2+ uptake when protein kinases are active.
  • This localized uptake prevents mitochondrial overload and protects against apoptosis.
  • The study presents a model explaining varying mitochondrial Ca2+ signals based on ER proximity and signaling pathways.