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

2.0K
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...
2.0K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.0K
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,...
3.0K
Mitochondrial Membranes01:45

Mitochondrial Membranes

6.6K
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,...
6.6K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

4.1K
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...
4.1K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

3.5K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
3.5K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.5K
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...
2.5K

You might also read

Related Articles

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

Sort by
Same author

Sulfite Dynamics Affect Drought Tolerance and Water Status in Arabidopsis and Tomato.

Journal of experimental botany·2026
Same author

A mitochondria-driven quality control mechanism for peroxisomal membrane proteins.

Nature communications·2026
Same author

Comprehensive Chemoproteomics Unveils Selective HMG-CoA Synthase 1 Inhibitors for Targeting Mevalonate Metabolism in Cancer.

Journal of the American Chemical Society·2026
Same author

Machine perception liquid biopsy identifies brain tumours via systemic immune and tumour microenvironment signature.

Nature nanotechnology·2025
Same author

STK405759 targets microtubules, modulates STAT1, and enhances ruxolitinib efficacy in myeloproliferative neoplasms.

American journal of cancer research·2025
Same author

Emerging dimensions of mitochondrial specialization.

Biological chemistry·2025

Related Experiment Video

Updated: May 10, 2025

Visualizing Mitophagy with Fluorescent Dyes for Mitochondria and Lysosome
07:56

Visualizing Mitophagy with Fluorescent Dyes for Mitochondria and Lysosome

Published on: November 30, 2022

4.1K

TOM20-driven E3 ligase recruitment regulates mitochondrial dynamics through PLD6.

Anat Raiff1, Shidong Zhao2, Aizat Bekturova1

  • 1Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel.

Nature Chemical Biology
|April 22, 2025
PubMed
Summary

The ubiquitin-proteasome system (UPS) regulates mitochondrial dynamics via FEM1B, which targets PLD6 for degradation. Disrupting this pathway causes mitochondrial defects, highlighting FEM1B

More Related Videos

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
08:27

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

1.5K
Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans
08:47

Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans

Published on: July 5, 2019

9.6K

Related Experiment Videos

Last Updated: May 10, 2025

Visualizing Mitophagy with Fluorescent Dyes for Mitochondria and Lysosome
07:56

Visualizing Mitophagy with Fluorescent Dyes for Mitochondria and Lysosome

Published on: November 30, 2022

4.1K
Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays
08:27

Visualization and Quantification of Endogenous Intra-Organelle Protein Interactions at ER-Mitochondria Contact Sites by Proximity Ligation Assays

Published on: October 20, 2023

1.5K
Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans
08:47

Quantitative Approaches for Studying Cellular Structures and Organelle Morphology in Caenorhabditis elegans

Published on: July 5, 2019

9.6K

Area of Science:

  • Cell Biology
  • Mitochondrial Biology
  • Molecular Mechanisms

Background:

  • Mitochondrial homeostasis relies on regulated fusion and fission dynamics.
  • The ubiquitin-proteasome system (UPS) is crucial for degrading mitochondrial proteins.
  • Dysregulation of mitochondrial dynamics is linked to various cellular pathologies.

Purpose of the Study:

  • To identify novel regulators of mitochondrial dynamics within the UPS.
  • To elucidate the role of cullin-RING E3 ligase 2 (CRL2) and FEM1B in mitochondrial regulation.
  • To investigate the interaction between FEM1B, PLD6, and TOM20 in maintaining mitochondrial morphology.

Main Methods:

  • Proteomic analysis to identify protein interactions and turnover.
  • Structural and biochemical assays to confirm physical interactions.
  • Genetic manipulation (ablation) and functional assays to assess mitochondrial defects.

Main Results:

  • FEM1B was identified as a substrate receptor that targets PLD6 for degradation.
  • FEM1B directly interacts with PLD6, and this interaction is mediated by TOM20.
  • FEM1B or FEM1B-TOM20 interaction disruption leads to impaired PLD6 degradation and mitochondrial dysfunction.

Conclusions:

  • FEM1B is a critical regulator of mitochondrial dynamics through PLD6 turnover.
  • The FEM1B-TOM20-PLD6 axis provides a new mechanism for UPS-mediated mitochondrial quality control.
  • Understanding these pathways offers insights into maintaining mitochondrial morphology and homeostasis.