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

Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

5.9K
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...
5.9K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

3.8K
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...
3.8K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

13.5K
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,...
13.5K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

18.0K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
18.0K
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

4.4K
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
4.4K
The Proteasome Structure01:17

The Proteasome Structure

2.0K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
2.0K

You might also read

Related Articles

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

Sort by
Same author

Recognition of small Tim chaperones by the mitochondrial Yme1 protease.

Protein science : a publication of the Protein Society·2026
Same author

Recognition of small Tim chaperones by the mitochondrial Yme1 protease.

bioRxiv : the preprint server for biology·2025
Same author

AAA+ proteins: converging mechanisms, diverging functions.

Nature structural & molecular biology·2020
Same author

Mitochondrial AAA proteases: A stairway to degradation.

Mitochondrion·2019
Same author

Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.

Molecular cell·2019
Same author

FABP1 controls hepatic transport and biotransformation of Δ<sup>9</sup>-THC.

Scientific reports·2019
Same journal

Mesenchymal stem cells-derived extracellular vesicles as a novel drug delivery carrier: engineering strategies and clinical safety estimation.

Frontiers in molecular biosciences·2026
Same journal

Preparation and analysis of tobacco glycosides, and the relationship between glycoside aglycones and pyrolysis products: a review.

Frontiers in molecular biosciences·2026
Same journal

Peritoneal metastasis in pancreatic cancer: molecular mechanisms, microenvironmental remodeling, and emerging intraperitoneal interventions.

Frontiers in molecular biosciences·2026
Same journal

Insights from LC-MS-based cerebrospinal fluid metabolomics in tuberculous meningitis.

Frontiers in molecular biosciences·2026
Same journal

Emerging roles of Notch signaling in the tumor microenvironment of digestive system cancers.

Frontiers in molecular biosciences·2026
Same journal

Adenosine metabolism as an endogenous protective mechanism in response to upstream ischemic injury.

Frontiers in molecular biosciences·2026
See all related articles

Related Experiment Video

Updated: Mar 1, 2026

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

3.0K

Multifunctional Mitochondrial AAA Proteases.

Steven E Glynn1

  • 1Department of Biochemistry and Cell Biology, Stony Brook UniversityStony Brook, NY, United States.

Frontiers in Molecular Biosciences
|June 8, 2017
PubMed
Summary
This summary is machine-generated.

Mitochondrial AAA proteases, i-AAA and m-AAA, maintain cell health by controlling protein levels. These essential proteases ensure proper mitochondrial function through degradation and remodeling of proteins.

Keywords:
AAA+i-AAAm-AAAmitochondriaproteolysis

More Related Videos

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
10:31

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

8.1K
Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

13.5K

Related Experiment Videos

Last Updated: Mar 1, 2026

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

3.0K
A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
10:31

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

8.1K
Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

13.5K

Area of Science:

  • Cellular Biology
  • Mitochondrial Biology
  • Biochemistry

Background:

  • Mitochondria are vital for eukaryotic cell survival, relying on protein homeostasis (proteostasis) for function.
  • Misfolded or damaged proteins disrupt mitochondrial activity, leading to severe human diseases.
  • ATP-driven AAA+ proteins are critical for maintaining mitochondrial proteostasis.

Purpose of the Study:

  • To review recent advances in understanding mitochondrial AAA proteases.
  • To elucidate the mechanisms of substrate recognition, handling, and degradation by these proteases.
  • To highlight the role of these proteases in controlling diverse mitochondrial activities.

Main Methods:

  • Review of current literature on mitochondrial AAA proteases.
  • Analysis of mechanisms for protein substrate recognition and processing.
  • Discussion of protease functions in protein biogenesis, quality control, and metabolic regulation.

Main Results:

  • Mitochondrial AAA proteases (i-AAA and m-AAA) are located on the inner mitochondrial membrane.
  • These proteases exhibit diverse substrate processing functions, including degradation, partial processing, and membrane dislocation.
  • Their actions impact protein biogenesis, quality control, and metabolic pathways within the mitochondria.

Conclusions:

  • Mitochondrial AAA proteases are key regulators of mitochondrial proteostasis.
  • Understanding their mechanisms is crucial for comprehending organellar function and disease development.
  • These proteases offer versatile strategies for controlling protein fate within the mitochondria.