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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

13.6K
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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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

5.1K
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.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

3.9K
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...
3.9K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

5.1K
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...
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Related Experiment Video

Updated: Mar 12, 2026

Analyzing Mitochondrial Transport and Morphology in Human Induced Pluripotent Stem Cell-Derived Neurons in Hereditary Spastic Paraplegia
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Analyzing Mitochondrial Transport and Morphology in Human Induced Pluripotent Stem Cell-Derived Neurons in Hereditary Spastic Paraplegia

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MITO-Porter for Mitochondrial Delivery and Mitochondrial Functional Analysis.

Yuma Yamada1, Hideyoshi Harashima2

  • 1Laboratory for Molecular Design of Pharmaceutics, Faculty of Pharmaceutical Sciences, Hokkaido University, Kita-12, Nishi-6, Kita-ku, Sapporo, 060-0812, Japan.

Handbook of Experimental Pharmacology
|November 11, 2016
PubMed
Summary

Researchers developed a novel MITO-Porter system for targeted mitochondrial drug delivery. This liposome-based carrier enables macromolecular cargo introduction into mitochondria, impacting disease therapy and life sciences.

Keywords:
MITO-PorterMembrane fusionMitochondriaMitochondrial drug deliveryMitochondrial functionMitochondrial gene therapyMitochondrial medicine development

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Isolation and Functional Analysis of Mitochondria from Cultured Cells and Mouse Tissue
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Author Spotlight: Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification

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Area of Science:

  • Mitochondrial biology
  • Drug delivery systems
  • Biotechnology

Background:

  • Mitochondria play crucial roles in cellular functions, health, and disease.
  • Targeted delivery of therapeutic agents to mitochondria is challenging but holds significant potential.
  • Existing mitochondrial drug delivery systems (DDSs) are limited.

Purpose of the Study:

  • To introduce a novel liposome-based carrier, the MITO-Porter, for efficient mitochondrial drug delivery.
  • To demonstrate the therapeutic potential of mitochondrial DDS in disease models.
  • To showcase the regulation of mitochondrial function through targeted delivery.

Main Methods:

  • Development of the MITO-Porter, a liposome-based carrier for macromolecular cargo.
  • Utilizing membrane fusion for cargo introduction into mitochondria.
  • Application of MITO-Porter in animal disease models and in vitro studies.

Main Results:

  • Demonstrated successful delivery of macromolecular cargoes into mitochondria using MITO-Porter.
  • Showcased the therapeutic efficacy of MITO-Porter in preclinical animal models of disease.
  • Achieved mitochondrial RNA knockdown and functional impact using antisense oligo-RNA delivered by MITO-Porter.

Conclusions:

  • The MITO-Porter represents a significant advancement in mitochondrial drug delivery systems.
  • Mitochondrial DDS hold promise for innovative therapeutic strategies and advancements in life sciences.
  • Targeted mitochondrial delivery enables precise regulation of mitochondrial function for therapeutic benefit.