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Related Concept Videos

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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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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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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An Improved Method to Isolate Mitochondrial Contact Sites
07:55

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Published on: June 16, 2023

Cyclophilin D modulates mitochondrial acetylome.

Tiffany Tuyen M Nguyen1, Renee Wong, Sara Menazza

  • 1From the Systems Biology Center (T.T.M.N., S.M., J.S., E.M.), Division of Cardiovascular Sciences (R.W.), Proteomics Core Facility (Y.C., G.W., M.G.), and Center for Molecular Medicine (M.N.S.), National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD; and Department of Pathology, Johns Hopkins Medical Center, Baltimore, MD (C.S.).

Circulation Research
|September 25, 2013
PubMed
Summary

Loss of cyclophilin D (CypD) alters cardiac mitochondrial acetylation, impacting fatty acid oxidation. This study reveals CypD's role in regulating the mitochondrial acetylome and cardiac metabolism.

Keywords:
acetylationcyclophilin Dmitochondriaproteomicssirtuin 3

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Area of Science:

  • Mitochondrial biology
  • Proteomics
  • Biochemistry

Background:

  • Mice lacking cyclophilin D (CypD) exhibit altered cardiac metabolism.
  • Protein acetylation is known to regulate metabolic pathways.
  • Investigating the role of acetylation in CypD-deficient hearts is crucial.

Purpose of the Study:

  • To test if the loss of CypD affects the cardiac mitochondrial acetylome.
  • To identify changes in protein acetylation in CypD knockout mouse hearts.
  • To understand the functional consequences of altered acetylation.

Main Methods:

  • Cardiac mitochondria isolated from wild-type and CypD(-/-) mice.
  • Tryptic digests analyzed using mass spectrometry after anti-acetyl lysine immunoprecipitation.
  • Label-free quantification to compare acetylation levels.

Main Results:

  • Significant alterations in the mitochondrial acetylome of CypD(-/-) mice were observed.
  • Increased acetylation of proteins involved in fatty acid and branched-chain amino acid metabolism.
  • Activity of l-3-hydroxyacyl-CoA dehydrogenase, a key enzyme in fatty acid oxidation, was inhibited by approximately 50% in CypD(-/-) mitochondria.

Conclusions:

  • Cyclophilin D plays a role in modulating protein acetylation within mitochondria.
  • Ablation of CypD leads to changes in the mitochondrial acetylome.
  • These acetylation changes may contribute to the altered mitochondrial metabolism observed in CypD(-/-) mice.