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Related Concept Videos

Mitochondrial Membranes01:45

Mitochondrial Membranes

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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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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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Structure of Porins01:21

Structure of Porins

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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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...
3.8K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

3.6K
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.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
3.6K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.8K
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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Related Experiment Video

Updated: Oct 15, 2025

Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
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Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess

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The mitochondrial permeability transition: Recent progress and open questions.

Paolo Bernardi1, Michela Carraro1, Giovanna Lippe2

  • 1Department of Biomedical Sciences and CNR Neuroscience Institute, University of Padova, Italy.

The FEBS Journal
|October 28, 2021
PubMed
Summary

The mitochondrial permeability transition pore (PTP), a Ca2+-dependent channel, is crucial for cell death and ion homeostasis. Recent research suggests F-ATP synthase or adenine nucleotide translocator (ANT) may form the PTP, offering new therapeutic targets.

Keywords:
ATP synthaseadenine nucleotide translocatorcalcium transportchannelscyclophilincyclosporinemitochondriapermeability transition

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Multi-parameter Measurement of the Permeability Transition Pore Opening in Isolated Mouse Heart Mitochondria
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Simultaneous Measurement of Mitochondrial Calcium and Mitochondrial Membrane Potential in Live Cells by Fluorescent Microscopy
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Area of Science:

  • Mitochondrial biology
  • Cellular physiology
  • Biochemistry

Background:

  • The mitochondrial permeability transition (MPT) is a Ca2+-dependent increase in inner mitochondrial membrane permeability, a process poorly understood for decades.
  • Initially dismissed, MPT is now recognized as a key regulator of mitochondrial ion homeostasis and a target for cell death modulation.
  • The MPT is mediated by the mitochondrial permeability transition pore (PTP), regulated by matrix cyclophilin D.

Purpose of the Study:

  • To review the structural basis and potential mechanisms of PTP formation by F-ATP synthase and adenine nucleotide translocator (ANT).
  • To synthesize current understanding and highlight controversies surrounding the molecular identity of the PTP.
  • To re-examine early findings on PTP modulation to guide future research.

Main Methods:

  • Structural analysis of ANT and F-ATP synthase.
  • Review of existing literature on PTP modulation and formation mechanisms.
  • Discussion of Ca2+-dependent conformational changes in mitochondrial proteins.

Main Results:

  • F-ATP synthase and ANT are proposed as key candidates for forming the PTP.
  • Evidence supporting and challenging the roles of F-ATP synthase and ANT in PTP formation is discussed.
  • Early studies on PTP modulation reveal intriguing findings requiring further investigation.

Conclusions:

  • The precise molecular composition of the PTP remains unresolved, with F-ATP synthase and ANT as leading hypotheses.
  • Further experimental investigation is needed to elucidate the exact mechanism of PTP opening.
  • Understanding the PTP is critical for its potential therapeutic targeting in cell death-related diseases.