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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,...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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...
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...

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Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
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Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission.

Sajjan Koirala1, Qian Guo, Raghav Kalia

  • 1Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 27, 2013
PubMed
Summary
This summary is machine-generated.

Mitochondrial fission relies on dynamin GTPases and adaptor proteins. Researchers found that specific adaptors, like MiDs, can alter dynamin structure, aiding in mitochondrial division.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitochondrial fission is crucial for cellular function and is mediated by dynamin-related GTPases (Dnm1/Drp1) and adaptor proteins.
  • Adaptor proteins (Fis1, Mdv1, Mff, MiDs) are known to recruit GTPases to the mitochondrial surface, but their role in membrane scission is unclear.

Purpose of the Study:

  • To determine the minimal combinations of GTPases and adaptors sufficient for mitochondrial fission.
  • To investigate the role of adaptor proteins in both GTPase recruitment and membrane scission.

Main Methods:

  • Utilized a yeast strain deficient in all known fission proteins.
  • Assessed mitochondrial fission using minimal combinations of GTPases and adaptors.
  • Performed in vitro co-assembly assays with Drp1 and MiDs.

Main Results:

  • Fis1 is dispensable for mitochondrial fission.
  • Membrane-anchored Mdv1, Mff, or MiDs, when paired with their respective GTPases, are sufficient for mitochondrial division.
  • MiDs coassemble with Drp1 in vitro, forming a heteropolymer with a narrower diameter than Drp1 homopolymers.

Conclusions:

  • Specific adaptor proteins, such as MiDs, are sufficient to mediate mitochondrial fission.
  • Adaptor proteins can directly alter the structural architecture of dynamin GTPase polymers.
  • This structural alteration by adaptors likely facilitates mitochondrial membrane constriction and scission.