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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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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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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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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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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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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 26, 2026

Simultaneous Measurement of Mitochondrial Calcium and Mitochondrial Membrane Potential in Live Cells by Fluorescent Microscopy
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MAVS-induced mitochondrial membrane remodeling.

Hector Flores-Romero1, Ana J García-Sáez1

  • 1Interfaculty Institute of Biochemistry, Eberhard Karls University, Tübingen, Germany.

The FEBS Journal
|April 9, 2019
PubMed
Summary
This summary is machine-generated.

Mitochondrial antiviral signal protein (MAVS) forms complexes during cellular stress. This study reveals MAVS-dependent mitochondrial morphology changes requiring its transmembrane domain are crucial for these processes.

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Area of Science:

  • Cellular biology
  • Mitochondrial dynamics
  • Innate immunity

Background:

  • Mitochondrial membrane remodeling is implicated in cell death and damage.
  • The precise mechanisms underlying mitochondrial remodeling remain unclear.
  • Mitochondrial antiviral signal protein (MAVS) plays a role in innate immunity.

Purpose of the Study:

  • To investigate the formation of macromolecular complexes of MAVS.
  • To understand the role of MAVS in mitochondrial morphology changes.
  • To elucidate the mechanisms of MAVS-mediated mitochondrial remodeling.

Main Methods:

  • Utilized super-resolution microscopy techniques.
  • Stimulated cells with double-stranded RNA (dsRNA).
  • Analyzed changes in mitochondrial morphology.

Main Results:

  • dsRNA stimulation correlated with MAVS-dependent alterations in mitochondrial morphology.
  • These morphological changes were dependent on the MAVS transmembrane domain.
  • MAVS forms macromolecular complexes during dsRNA stimulation.

Conclusions:

  • MAVS-mediated mitochondrial remodeling is essential for cellular responses to dsRNA.
  • The transmembrane domain of MAVS is critical for its function in mitochondrial morphology.
  • This study provides insights into the mechanisms of MAVS-driven mitochondrial changes.