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

11.7K
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,...
11.7K
The Proteasome01:13

The Proteasome

1.5K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.5K
The Proteasome02:18

The Proteasome

9.9K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
9.9K
The Proteasome02:18

The Proteasome

4.2K
4.2K
Mitochondrial Membranes01:45

Mitochondrial Membranes

16.4K
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,...
16.4K
Mitochondria01:37

Mitochondria

19.3K
Mitochondria are eukaryotic cellular organelles that are known to produce energy through a process called oxidative phosphorylation. Besides their primary function, mitochondria are involved in various cellular processes, including cell growth, differentiation, signaling, metabolism, and senescence. Age-related changes cause a decline in mitochondrial quality and integrity due to increased mitochondrial mutations and oxidative damage. Thus, aging can severely impact mitochondrial functions,...
19.3K

You might also read

Related Articles

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

Sort by
Same author

IRE1 regulates the proteostasis of TDP-43/TARDBP in ALS/FTD through ribosome-associated quality control.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

EZH2 as regulator of stemness signature and driver of esophageal squamous cell carcinomas.

Scientific reports·2026
Same author

Mitochondrial complex I as a master regulator of redox signaling: From structural architecture to directionality of electron transport.

Free radical biology & medicine·2026
Same author

Tau-induced mitochondrial reverse electron transport drives neurodegeneration.

bioRxiv : the preprint server for biology·2026
Same author

Extension of Lifespan and Amelioration of Alzheimer's Disease Phenotypes by Genetic Manipulation of Mitochondrial NAD<sup>+</sup>/NADH Ratio.

Aging and disease·2026
Same author

Small target detection of floating objects in river channels based on improved YOLOv7.

Scientific reports·2026
Same journal

Horizontal transfer of mitochondria in cancer: The physiology reborn in disease?

Trends in cell biology·2026
Same journal

Spindle errors: A stress test for epithelial robustness.

Trends in cell biology·2026
Same journal

Multicellular ecosystems: Linking cellular diversity to tissue function and disease.

Trends in cell biology·2026
Same journal

Orchestrating the signaling-bias at the protease-activated receptor, PAR1.

Trends in cell biology·2026
Same journal

Crashing by design: Utilizing DNA damage for MCC differentiation.

Trends in cell biology·2026
Same journal

The value of a shared lab: Our insights.

Trends in cell biology·2026
See all related articles

Related Experiment Video

Updated: Dec 25, 2025

Assessing Mitochondrial Function in Sciatic Nerve by High-Resolution Respirometry
08:19

Assessing Mitochondrial Function in Sciatic Nerve by High-Resolution Respirometry

Published on: May 5, 2022

2.7K

Mechanisms Linking Mitochondrial Dysfunction and Proteostasis Failure.

Bingwei Lu1, Su Guo2

  • 1Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.

Trends in Cell Biology
|March 24, 2020
PubMed
Summary
This summary is machine-generated.

Cellular protein homeostasis (proteostasis) declines with age, contributing to neurodegenerative diseases. Mitochondrial dysfunction links to proteostasis failure through aberrant protein production, offering new therapeutic targets.

Keywords:
CAT-tailingMISTERMINATEco-translational mitochondrial importmitochondrial dysfunctionprotein homeostasis (proteostasis)ribosome-associated quality control

More Related Videos

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

3.2K
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

2.8K

Related Experiment Videos

Last Updated: Dec 25, 2025

Assessing Mitochondrial Function in Sciatic Nerve by High-Resolution Respirometry
08:19

Assessing Mitochondrial Function in Sciatic Nerve by High-Resolution Respirometry

Published on: May 5, 2022

2.7K
Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

3.2K
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

2.8K

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Neuroscience

Background:

  • Cellular protein homeostasis (proteostasis) is crucial for eukaryotic life.
  • Proteostasis failure is linked to aging and age-related diseases, particularly neurodegenerative disorders.
  • The precise mechanisms underlying proteostasis failure remain incompletely understood.

Purpose of the Study:

  • To review recent findings on mitochondrial outer membrane (MOM)-associated mRNA translation.
  • To explore the link between mitochondrial function and proteostasis.
  • To discuss the generation of aberrant proteins and their implications for human diseases.

Main Methods:

  • Literature review of model organism studies (yeast, Drosophila).
  • Examination of ribosome-associated quality control (RQC) mechanisms.
  • Analysis of aberrant protein generation, including C-terminal extensions (CTEs).

Main Results:

  • Mitochondrial outer membrane (MOM)-associated translation is sensitive to mitochondrial dysfunction.
  • Ribosome-associated quality control (RQC) surveils this process.
  • Defects lead to aberrant proteins with C-terminal extensions (CTEs), promoting aggregation and proteostasis failure.

Conclusions:

  • Mitochondrial dysfunction can directly impair proteostasis via altered mRNA translation.
  • Aberrant protein production, specifically CTEs, is a key mechanism driving proteostasis failure.
  • Understanding these pathways offers potential therapeutic strategies for age-related diseases.