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

The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

3.2K
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...
3.2K
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
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

2.7K
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...
2.7K
Structure of Porins01:21

Structure of Porins

2.8K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
2.8K
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

3.6K
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...
3.6K

You might also read

Related Articles

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

Sort by
Same author

Gene-editing in patient and humanized-mice primary muscle stem cells rescues dysferlin expression in dysferlin-deficient muscular dystrophy.

Nature communications·2025
Same author

Coordination of cytochrome bc<sub>1</sub> complex assembly at MICOS.

EMBO reports·2024
Same author

Identification of drug-like molecules targeting the ATPase activity of dynamin-like EHD4.

PloS one·2024
Same author

Structure-based humanization of a therapeutic antibody for multiple myeloma.

Journal of molecular medicine (Berlin, Germany)·2024
Same author

Pathogenic mutations of human phosphorylation sites affect protein-protein interactions.

Nature communications·2024
Same author

Author Correction: GIMAP5 deficiency reveals a mammalian ceramide-driven longevity assurance pathway.

Nature immunology·2024

Related Experiment Video

Updated: May 16, 2025

Studying Mitochondrial Structure and Function in Drosophila Ovaries
09:53

Studying Mitochondrial Structure and Function in Drosophila Ovaries

Published on: January 4, 2017

23.9K

Molecular machineries shaping the mitochondrial inner membrane.

Oliver Daumke1,2, Martin van der Laan3

  • 1Structural Biology, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany. oliver.daumke@mdc-berlin.de.

Nature Reviews. Molecular Cell Biology
|May 14, 2025
PubMed
Summary

Mitochondrial inner membranes form cristae essential for cell function. Protein machines like MICOS and OPA1 control their shape and fusion, with mutations impacting mitochondrial health.

More Related Videos

Author Spotlight: Decoding Mitochondrial Aging
08:48

Author Spotlight: Decoding Mitochondrial Aging

Published on: June 30, 2023

3.5K
Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
07:55

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights

Published on: June 16, 2023

1.3K

Related Experiment Videos

Last Updated: May 16, 2025

Studying Mitochondrial Structure and Function in Drosophila Ovaries
09:53

Studying Mitochondrial Structure and Function in Drosophila Ovaries

Published on: January 4, 2017

23.9K
Author Spotlight: Decoding Mitochondrial Aging
08:48

Author Spotlight: Decoding Mitochondrial Aging

Published on: June 30, 2023

3.5K
Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
07:55

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights

Published on: June 16, 2023

1.3K

Area of Science:

  • Cell Biology
  • Mitochondrial Biology
  • Structural Biology

Background:

  • Mitochondria possess intricate inner membrane invaginations called cristae, crucial for oxidative phosphorylation and biosynthesis.
  • Protein complexes, including F1Fo-ATP synthase and MICOS, act as scaffolds for mitochondrial inner membrane (MIM) biogenesis and remodeling.
  • The dynamin-like GTPase OPA1 regulates cristae architecture and MIM fusion.

Purpose of the Study:

  • To review the cooperative mechanisms of MIM-shaping machineries in controlling cristae dynamics.
  • To discuss the role of these machineries in MIM fusion and cellular signaling.
  • To explore the consequences of mutations in MIM-shaping proteins on mitochondrial function.

Main Methods:

  • Review of recent structural and functional studies on mitochondrial protein machineries.
  • Analysis of signaling pathways influencing cristae architecture and dynamics.
  • Integration of data on the impact of genetic mutations on mitochondrial function.

Main Results:

  • Recent structural insights have significantly advanced the understanding of mitochondrial nano-machineries.
  • MIM-shaping machineries cooperate to regulate cristae and crista junction dynamics, including fusion.
  • Signal-dependent rearrangements and fusion events are governed by OPA1.

Conclusions:

  • Cooperation between protein machineries is key to mitochondrial inner membrane architecture and function.
  • Dysfunctional MIM-shaping machineries, due to mutations, compromise essential mitochondrial processes.
  • Understanding these dynamics offers insights into mitochondrial diseases and potential therapeutic targets.