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Related Concept Videos

Mitochondrial Membranes01:45

Mitochondrial Membranes

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,...
Mitochondrial Membranes01:45

Mitochondrial Membranes

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,...
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...
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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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,...
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...

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Related Experiment Video

Updated: Jun 23, 2026

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria
09:01

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Published on: January 7, 2022

Mitochondrial-derived compartments buffer outer membrane protein load during acute mitochondrial adaptation.

Bo J Price, Sai Sangeetha Balasubramaniam, Adam L Hughes

    Biorxiv : the Preprint Server for Biology
    |June 22, 2026
    PubMed
    Summary

    Mitochondria-derived compartments (MDCs) form during metabolic stress to manage protein overload. These structures help the outer mitochondrial membrane adapt by buffering new proteins before the organelle fully adjusts.

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    Area of Science:

    • Cellular Biology
    • Mitochondrial Dynamics
    • Metabolic Adaptation

    Background:

    • Cells rapidly remodel mitochondria during metabolic transitions, involving proteome expansion and reorganization.
    • The mechanism by which the outer mitochondrial membrane (OMM) accommodates increased protein synthesis during acute mitochondrial biogenesis is unclear.

    Purpose of the Study:

    • To investigate the formation and function of mitochondrial-derived compartments (MDCs) during metabolic stress.
    • To elucidate the molecular requirements for MDC formation and their role in outer mitochondrial membrane adaptation.

    Main Methods:

    • Induction of metabolic perturbations (glucose restriction, carbon-source switching, salt stress) in cell models.
    • Analysis of MDC formation using microscopy and biochemical assays.
    • Genetic manipulation to assess the roles of Snf1 kinase and Mig1 repressor in MDC induction.
    • Investigation of mitochondrial protein targeting and import pathways.

    Main Results:

    • Mitochondrial-derived compartments (MDCs), multilamellar domains budding from the OMM, arise during metabolic perturbations.
    • MDC formation requires the energy-sensing kinase Snf1 and derepression of Mig1, linking them to increased mitochondrial protein synthesis.
    • MDC induction can be triggered by activating mitochondrial biogenesis independently of metabolic changes.
    • Disrupting protein import into mitochondria prevents MDC formation and leads to cargo mislocalization.

    Conclusions:

    • Mitochondrial-derived compartments (MDCs) function as adaptive domains that buffer the outer mitochondrial membrane protein load during adaptation.
    • MDCs play a crucial role in maintaining outer membrane homeostasis under conditions of increased protein synthesis.
    • These findings support a model where MDCs are integral to the cell's response to metabolic stress and mitochondrial biogenesis.