Jove
Visualize
Contact Us

Related Concept Videos

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 Protein Sorting01:39

Mitochondrial Protein Sorting

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...
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

Surgical Outcomes of Revision Meniscal Repair: A Case Series.

Orthopaedic journal of sports medicine·2026
Same author

Integrated interpretation of exercise electrocardiography and cardiopulmonary exercise testing for detection of significant coronary artery stenosis.

Journal of cardiology·2026
Same author

Clinical outcomes of hybrid closed-wedge high tibial osteotomy according to the Kellgren-Lawrence grade.

The Knee·2026
Same author

Fatal retroperitoneal fungal abscess following surgery for gallbladder cancer: an autopsy case report.

Journal of surgical case reports·2026
Same author

Predictive Nomogram for Recurrence After Upfront Surgery for Resectable Pancreatic Ductal Adenocarcinoma: A Multicenter Study (OS-HBP-2).

Cancers·2026
Same author

Prognosis Prediction Model After Upfront Surgery for Resectable Pancreatic Ductal Adenocarcinoma: A Multicenter Study (OS-HBP-2).

Cancers·2025
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 Experiment Video

Updated: Jul 16, 2026

Understanding the Changes in Mitochondrial Morphology through Dynamic and Three-dimensional Fluorescence Micrographs
08:15

Understanding the Changes in Mitochondrial Morphology through Dynamic and Three-dimensional Fluorescence Micrographs

Published on: August 15, 2025

Human Misato regulates mitochondrial distribution and morphology.

Masashi Kimura1, Yukio Okano

  • 1Department of Molecular Pathobiochemistry, Division of Disease Control, Gifu University Graduate School of Medicine, Yanagido 1-1, Gifu 501-1194, Japan. yo@gifu-u.ac.jp

Experimental Cell Research
|March 14, 2007
PubMed
Summary

Human Misato protein is crucial for mitochondrial structure and function. Its depletion causes cell death, while overexpression leads to abnormal mitochondrial distribution and reduced cell viability, highlighting its regulatory role.

More Related Videos

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models
08:48

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models

Published on: June 30, 2023

Related Experiment Videos

Last Updated: Jul 16, 2026

Understanding the Changes in Mitochondrial Morphology through Dynamic and Three-dimensional Fluorescence Micrographs
08:15

Understanding the Changes in Mitochondrial Morphology through Dynamic and Three-dimensional Fluorescence Micrographs

Published on: August 15, 2025

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models
08:48

Using Live Cell STED Imaging to Visualize Mitochondrial Inner Membrane Ultrastructure in Neuronal Cell Models

Published on: June 30, 2023

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Misato proteins are conserved GTPase family members found in various organisms.
  • Human Misato shares homology with Drosophila melanogaster Misato and yeast DML1.
  • Understanding human Misato's function is essential for comprehending mitochondrial dynamics.

Purpose of the Study:

  • To characterize the function of human Misato.
  • To investigate human Misato's role in mitochondrial morphology and distribution.
  • To determine the consequences of Misato dysregulation on cell viability.

Main Methods:

  • Tissue distribution analysis of human Misato.
  • Subcellular localization studies using immunofluorescence and mitochondrial fractionation.
  • RNA interference (siRNA) to deplete Misato expression in HeLa cells.
  • Overexpression studies using EGFP-Misato in COS-7 cells.

Main Results:

  • Human Misato is ubiquitously distributed and localized to the mitochondrial outer membrane.
  • Misato depletion resulted in mitochondrial fragmentation, growth deficiency, and apoptosis.
  • Misato overexpression caused perinuclear mitochondrial aggregation and severe defects in cell viability and nuclear structure.

Conclusions:

  • Human Misato plays a critical role in maintaining mitochondrial fusion, distribution, and morphology.
  • Unregulated expression of Misato leads to significant cellular dysfunction and death.
  • Misato is a key regulator of mitochondrial homeostasis.