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

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...
Structure of Porins01:21

Structure of Porins

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 precursors...
Anaphase A and B01:39

Anaphase A and B

Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
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...
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular cargos...
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...

You might also read

Related Articles

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

Sort by
Same author

Hetero-oligomerization drives structural plasticity of eukaryotic peroxiredoxins.

Nature chemical biology·2026
Same author

Identification of the Subcompartment-Specific Mitochondrial Proteome by APEX2 Proximity Labeling in <i>Saccharomyces cerevisiae</i>.

Bio-protocol·2026
Same author

Mrx6 binds the Lon protease Pim1 N-terminal domain to confer selective substrate specificity and regulate mtDNA copy number.

Nucleic acids research·2026
Same author

Don't forget protein synthesis! Mitochondria of cancer cells import glutamine to fuel metabolism and to charge tRNAs for translation.

Molecular cell·2026
Same author

The ribosome-associated complex regulates cytosolic translation upon mitoprotein-induced stress.

The FEBS journal·2025
Same author

The IQ-compete assay for measuring mitochondrial protein import efficiencies in living yeast cells.

FEBS letters·2025

Related Experiment Video

Updated: May 28, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

MINOS is plus: a Mitofilin complex for mitochondrial membrane contacts.

Johannes M Herrmann1

  • 1Cell Biology, University of Kaiserslautern, Erwin-Schrödinger-Strasse 13, 67663 Kaiserslautern, Germany. hannes.herrmann@biologie.uni-kl.de

Developmental Cell
|October 22, 2011
PubMed
Summary

The MINOS complex organizes cristae junctions, defining respiratory compartments in the inner mitochondrial membrane. Its central component, mitofilin, also links the inner and outer mitochondrial membranes for protein import.

More Related Videos

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

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

Related Experiment Videos

Last Updated: May 28, 2026

An Improved Method to Isolate Mitochondrial Contact Sites
07:55

An Improved Method to Isolate Mitochondrial Contact Sites

Published on: June 16, 2023

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

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

Area of Science:

  • Mitochondrial biology
  • Cellular structure
  • Protein import

Background:

  • Cristae junctions delineate functional respiratory compartments within the inner mitochondrial membrane.
  • Understanding the molecular machinery that organizes these junctions is crucial for mitochondrial function.

Discussion:

  • The MINOS complex, a novel assembly, has been identified as a key organizer of cristae junctions.
  • Mitofilin/Fcj1 is the central protein within the MINOS complex, playing a pivotal role in its structure and function.

Key Insights:

  • The MINOS complex establishes the structural organization of cristae junctions.
  • Mitofilin/Fcj1 acts as a bridge, connecting the inner mitochondrial membrane to the outer membrane protein import machinery.

Outlook:

  • Further investigation into the MINOS complex could reveal new therapeutic targets for mitochondrial diseases.
  • Elucidating the precise mechanisms of MINOS-mediated protein import may offer insights into mitochondrial dynamics and biogenesis.