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Related Concept Videos

Mitochondrial Membranes01:45

Mitochondrial Membranes

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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,...
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The Inner Mitochondrial Membrane01:28

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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...
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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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.
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Peroxisomes and mitochondria are two important oxygen-utilizing organelles in eukaryotic cells. Mitochondria carry out cellular respiration—the process that converts energy from food into ATP. Peroxisomes carry out a variety of functions, primarily breaking down different substances, such as fatty acids.
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Related Experiment Video

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Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
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Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights

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The mitochondria-plasma membrane contact site.

Benedikt Westermann1

  • 1Institut für Zellbiologie, Universität Bayreuth, Bayreuth 95440, Germany.

Current Opinion in Cell Biology
|March 25, 2015
PubMed
Summary

The Num1/Mdm36 complex tethers mitochondria to the cell cortex in yeast, influencing organelle distribution during cell division and dynamics. Similar mechanisms may operate in mammalian cells.

Area of Science:

  • Cell Biology
  • Mitochondrial Dynamics
  • Organelle Interactions

Background:

  • Mitochondria are dynamic organelles crucial for cellular function.
  • Their movement, fusion, and division are complex processes.
  • Interactions with other cellular structures significantly influence mitochondrial behavior.

Purpose of the Study:

  • To review the recently discovered Num1/Mdm36 complex.
  • To elucidate its role in tethering mitochondria to the plasma membrane in budding yeast.
  • To discuss its implications for mitochondrial distribution and dynamics during cell division.

Main Methods:

  • Molecular analysis of the Num1/Mdm36 complex in budding yeast.
  • Investigating the interaction between mitochondria and the cell cortex.

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  • Reviewing recent evidence on mitochondrial-plasma membrane tethering.

    • Main Results:

    • The Num1/Mdm36 complex anchors mitochondria to the cell cortex.
    • This tethering ensures retention of mitochondria in mother cells during division.
    • The complex integrates mitochondrial dynamics with cellular architecture.

    Conclusions:

    • The Num1/Mdm36 complex plays a key role in yeast mitochondrial inheritance and dynamics.
    • This mechanism highlights the importance of organelle-cell structure interactions.
    • Similar mitochondrial tethering mechanisms are suggested to exist in mammalian cells.