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This method exploits the contribution of the mitochondrial permeability transition pore to low-conductance proton leak to determine the voltage threshold for pore opening in neonatal fragile X syndrome mice with increased cardiomyocyte mitochondrial coenzyme Q content compared to wildtype control.
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Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
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Related Experiment Video

Updated: Jan 19, 2026

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
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Gasdermins: novel mitochondrial pore-forming proteins.

Corey Rogers1, Emad S Alnemri1

  • 1Department of Biochemistry and Molecular Biology, Sidney Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA.

Molecular & Cellular Oncology
|September 19, 2019
PubMed
Summary

Gasdermin proteins, known for cell membrane pore formation, can also permeabilize mitochondria. This mitochondrial permeabilization enhances apoptotic signaling, impacting cancer and hearing loss research.

Keywords:
DFNA5GSDMDGSDMEGasderminapoptosiscaspase-3cytochrome cinflammasomemitochondriapyroptosis

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Gasdermin proteins are primarily known for inducing pyroptosis via plasma membrane pore formation.
  • Their role in organelle interactions and other cell death pathways remains largely unexplored.

Purpose of the Study:

  • To investigate the role of gasdermin proteins beyond plasma membrane permeabilization.
  • To determine if gasdermin proteins interact with and permeabilize other organelles, specifically mitochondria.
  • To elucidate the functional consequences of mitochondrial permeabilization by gasdermins in cellular signaling.

Main Methods:

  • Utilized biochemical assays to detect protein-protein interactions.
  • Employed cell-based models to study gasdermin localization and function.
  • Assessed mitochondrial integrity and apoptotic signaling pathways using molecular biology techniques.

Main Results:

  • Demonstrated that certain gasdermin proteins can permeabilize the mitochondrial membrane.
  • Showed that mitochondrial permeabilization by gasdermins augments apoptotic signaling.
  • Identified a novel mechanism by which gasdermins contribute to cell death.

Conclusions:

  • Gasdermin proteins possess a dual function, impacting both plasma membrane and mitochondrial integrity.
  • Mitochondrial permeabilization by gasdermins represents a new avenue for understanding cell death.
  • These findings have potential implications for therapeutic strategies in cancer and hearing loss.