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Related Concept Videos

Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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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...
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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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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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Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

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Patterns of Mitochondrial ATP Predict Tissue Folding.

Bezia Lemma1, Megan Rothstein2, Pengfei Zhang1,3

  • 1Departments of Chemical & Biological Engineering, Princeton University, Princeton, NJ 08544.

Biorxiv : the Preprint Server for Biology
|September 5, 2025
PubMed
Summary
This summary is machine-generated.

During embryonic development, mitochondria fuel tissue folding by concentrating energy where needed. This localized energy production is conserved across species and essential for forming complex shapes.

Keywords:
Energy metabolismglycolysismechanical stressreaction-diffusion modelingtissue morphodynamics

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Area of Science:

  • Developmental Biology
  • Cellular Bioenergetics
  • Tissue Morphogenesis

Background:

  • Embryonic development relies on coordinated gene expression and mechanical forces.
  • Cellular energy, primarily from adenosine triphosphate (ATP) hydrolysis, powers these developmental processes.
  • Apical constriction is a fundamental mechanism for epithelial tissue folding across the animal kingdom.

Purpose of the Study:

  • To investigate the spatial patterning of chemical energy during embryonic tissue morphogenesis.
  • To determine the role of mitochondria in apical constriction and tissue folding.
  • To explore the conservation and predictive power of bioenergetic patterns in development.

Main Methods:

  • Utilized timelapse imaging to observe cellular dynamics during morphogenesis.
  • Employed spatial transcriptomics to map gene expression and cellular states.
  • Measured oxygen consumption rates to quantify cellular energy production.
  • Inhibited oxidative phosphorylation to assess its impact on tissue folding.

Main Results:

  • Mitochondria are enriched apically in epithelial cells during apical constriction.
  • Increased mitochondrial density, membrane potential, and ATP levels precede actomyosin contraction and tissue folding.
  • Inhibition of oxidative phosphorylation prevents tissue folding, highlighting its necessity.
  • Mitochondrial enrichment patterns are conserved in flies, chicks, and mice.

Conclusions:

  • Localized mitochondrial activity and ATP production are critical for driving apical constriction.
  • Spatial bioenergetics is a key, conserved feature of embryonic morphogenesis.
  • Subcellular energy patterns can predict tissue folding dynamics.