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

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,...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...
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...
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,...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...

You might also read

Related Articles

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

Sort by
Same author

Atmospheric Oxidation Kinetics of Monochloramine by Hydroxyl Radical, Carbonyl Oxide, and Sulfur Trioxide Catalyzed by Water.

The journal of physical chemistry. A·2026
Same author

Global trends in chronic kidney disease related cognitive impairment/dementia: a bibliometric analysis (2005-2025).

Frontiers in neurology·2026
Same author

PCS2-Based Schemes for Geometry Optimization and Frequency Calculations in Criegee Intermediate-Water Reactions.

The journal of physical chemistry. A·2026
Same author

Hybridndiff-UQ: Uncertainty quantification for hybrid neural differentiable modeling.

Theoretical and applied mechanics letters·2026
Same author

CoNFiLD-inlet: Synthetic turbulence inflow using generative latent diffusion models with neural fields.

Physical review fluids·2026
Same author

[Explanation and interpretation of pediatric blood requirement recommendations in the national health standard "Guideline for pediatric transfusion"].

Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics·2026
Same journal

Demonstration of a quantum C-NOT gate in a time-multiplexed fully reconfigurable photonic processor.

Nature communications·2026
Same journal

Nonlinear quantum light source with van der Waals ferroelectric NbOX<sub>2</sub> (X = Br, I).

Nature communications·2026
Same journal

Antagonistic histone H2A variants and autonomous heterochromatin formation shape epigenomic patterns in Arabidopsis.

Nature communications·2026
Same journal

The long tail of nitrate pollution in groundwater challenges governance of global water quality.

Nature communications·2026
Same journal

Select microbial metabolites promote tau aggregation in a murine tauopathy model.

Nature communications·2026
Same journal

Warming climate has lengthened global intense tropical cyclone seasons.

Nature communications·2026
See all related articles

Related Experiment Video

Updated: May 23, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

miR-484 regulates mitochondrial network through targeting Fis1.

Kun Wang1, Bo Long, Jian-Qin Jiao

  • 1Division of Cardiovascular Research, State Key Laboratory of Biomembrane and Membrane Biotechnology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China.

Nature Communications
|April 19, 2012
PubMed
Summary
This summary is machine-generated.

MicroRNA-484 (miR-484) inhibits mitochondrial fission by suppressing the translation of Fis1 protein. This finding reveals a novel regulatory pathway for mitochondrial dynamics and disease.

More Related Videos

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

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

Related Experiment Videos

Last Updated: May 23, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

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

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

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Mitochondria are vital organelles that maintain cellular health through fusion and fission.
  • Dysregulated mitochondrial fission is implicated in various diseases, but its regulatory mechanisms are not fully understood.

Purpose of the Study:

  • To investigate the role of microRNA-484 (miR-484) in regulating mitochondrial fission.
  • To elucidate the mechanism by which miR-484 affects mitochondrial fission and apoptosis.

Main Methods:

  • Investigated the interaction between miR-484 and Fis1 mRNA using molecular biology techniques.
  • Assessed the effects of miR-484 and Fis1 on mitochondrial fission and apoptosis in cell cultures (cardiomyocytes and adrenocortical cancer cells).
  • Utilized transgenic and knockout mouse models to study the in vivo function of Foxo3a and miR-484 in myocardial infarction.

Main Results:

  • miR-484 directly suppresses the translation of mitochondrial fission protein Fis1.
  • miR-484 inhibits Fis1-mediated mitochondrial fission and apoptosis in cardiomyocytes and cancer cells.
  • Fis1 is upregulated during anoxia, while miR-484 is downregulated, suggesting a role in stress response.
  • Foxo3a acts as a transactivator of miR-484 expression.
  • Foxo3a manipulation in mice altered miR-484 levels, mitochondrial fission, apoptosis, and myocardial infarction.

Conclusions:

  • miR-484 is a key regulator of mitochondrial fission and apoptosis by targeting Fis1.
  • The Foxo3a-miR-484 axis plays a critical role in controlling mitochondrial dynamics and cellular fate.
  • This microRNA-mediated pathway offers potential therapeutic targets for diseases associated with abnormal mitochondrial fission.