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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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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,...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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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.
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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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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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.
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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

The Inner Mitochondrial Membrane

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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 Precursor Proteins01:39

Mitochondrial Precursor Proteins

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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...
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Mfi2: an outer mitochondrial membrane mitofissin required for mitophagy.

Kentaro Furukawa1, Tatsuro Maruyama2, Yuji Sakai3

  • 1Department of Cellular Physiology, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.

Autophagy Reports
|March 6, 2026
PubMed
Summary

Mitophagy requires mitochondrial fragmentation, but traditional fission factors are dispensable. New research reveals mitofissins, proteins on mitochondrial membranes, drive this essential fission process independently of Dnm1.

Keywords:
Atg44Dnm1Mfi2mitochondrial fissionmitofissinmitophagy

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In Vitro and In Vivo Detection of Mitophagy in Human Cells, C. Elegans, and Mice

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • Mitophagy maintains cellular health by removing damaged mitochondria.
  • Mitochondrial fragmentation is crucial for mitophagy but its mechanism is unclear.
  • Known fission factors like Dnm1 are not essential for mitophagy.

Purpose of the Study:

  • To investigate the mechanism of mitochondrial fission during mitophagy.
  • To identify novel proteins involved in mitophagy-associated mitochondrial fragmentation.
  • To understand the role of mitofissins in mitophagy.

Main Methods:

  • Genetic analysis in yeast Saccharomyces cerevisiae.
  • Identification and characterization of mitochondrial outer membrane proteins.
  • Investigating protein function independently of Dnm1.

Main Results:

  • Mitofissins, a new class of proteins, are involved in mitochondrial fission during mitophagy.
  • Mitochondrial outer membrane protein Mfi2 (mitofissin 2) is essential for efficient mitophagy.
  • Mitofissin activity from both inner and outer mitochondrial membranes drives mitophagy-associated fission.

Conclusions:

  • Mitophagy-associated mitochondrial fission is mediated by mitofissins.
  • This process is independent of the canonical Dnm1 fission pathway.
  • Regulation of mitofissin activity and modulation by cardiolipin are key areas for future research.