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Related Concept Videos

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 Membranes01:45

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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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Protein Transport into the Inner Mitochondrial Membrane01:34

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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.
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Porin Insertion in the Outer Mitochondrial Membrane01:12

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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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Contact-dependent Signaling01:19

Contact-dependent Signaling

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Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
Gap Junctions
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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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Updated: Feb 16, 2026

Author Spotlight: Unveiling Mitochondrial Contact Sites and Architectural Insights
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BRD4-mediated ER membrane contact creates functionally distinct mitochondrial subtypes.

Brandon Chen1, Drew C Stark2, Pankaj V Jadhav3

  • 1Cellular and Molecular Biology Program, University of Michigan Medical School, Ann Arbor, MI 48109, USA; Department of Molecular & Integrative Physiology, University of Michigan, Ann Arbor, MI 48109, USA.

Molecular Cell
|February 14, 2026
PubMed
Summary
This summary is machine-generated.

Researchers discovered fedratinib, a drug that rapidly controls endoplasmic reticulum and mitochondria contact sites (ERMCSs) by inhibiting BRD4. This finding reveals a new epigenetic pathway impacting cellular metabolism.

Keywords:
bromodomain proteinendoplasmic reticulum-mitochondria contact siteshigh-throughput screeningmitochondrial electron transport chain

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Area of Science:

  • Cell Biology
  • Epigenetics
  • Metabolic Regulation

Background:

  • Inter-organellar communication is vital for cellular metabolism.
  • Endoplasmic reticulum and mitochondria contact sites (ERMCSs) are key sites of interaction.
  • Current tools lack temporal control for studying ERMCS regulation.

Purpose of the Study:

  • To identify novel tools for temporal control of ERMCSs.
  • To elucidate the mechanisms and metabolic roles of ERMCS regulation.
  • To uncover new signaling pathways connecting ERMCSs and metabolism.

Main Methods:

  • Drug screening to identify modulators of ERMCS abundance.
  • Utilized fedratinib, an FDA-approved drug targeting BRD4.
  • Assessed effects on mitochondrial and ER morphology, metabolic homeostasis, and electron transport chain function.

Main Results:

  • Fedratinib dramatically increases ERMCS abundance by inhibiting BRD4.
  • Fedratinib rapidly and reversibly modulates organelle morphology and metabolic homeostasis.
  • ERMCS modulation is dependent on mitochondrial electron transport chain complex III.

Conclusions:

  • Fedratinib provides a tool for temporal control of ERMCSs.
  • A novel epigenetic pathway involving BRD4 regulates ERMCSs.
  • This pathway connects ERMCSs to cellular metabolism, offering new therapeutic targets.