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Related Concept Videos

Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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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.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
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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.
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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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The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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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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Related Experiment Video

Updated: Feb 24, 2026

Neuromodulation and Mitochondrial Transport: Live Imaging in Hippocampal Neurons over Long Durations
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Melatonin transport into mitochondria.

Juan C Mayo1,2, Rosa M Sainz3,4, Pedro González-Menéndez3,4

  • 1Departamento de Morfología y Biología Celular, Facultad de Medicina, Universidad de Oviedo, C/Julián Clavería, 6, 33006, Oviedo, Asturias, Spain. mayojuan@uniovi.es.

Cellular and Molecular Life Sciences : CMLS
|August 23, 2017
PubMed
Summary
This summary is machine-generated.

Melatonin, a nighttime hormone, is a potent antioxidant with diverse functions, including neuroprotection and tumor suppression. New research highlights its transport into cells via glucose and peptide transporters, impacting mitochondrial actions.

Keywords:
DiffusionGLUT transportersMTNRMelatoninMitochondriaUptake

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Melatonin is a ubiquitous indoleamine produced nocturnally, involved in circadian rhythms, seasonal adaptation, and immune modulation.
  • Its antioxidant and neuroprotective properties are well-established, with mitochondria identified as key targets.
  • Melatonin exerts functions via direct radical scavenging and binding to membrane and nuclear receptors.

Purpose of the Study:

  • To explore the significance of newly discovered melatonin cellular uptake mechanisms.
  • To investigate the role of glucose transporters (GLUT/SLC2A) and oligopeptide transporters (PEPT1/2) in melatonin's actions.
  • To discuss the implications of active transport versus passive diffusion for melatonin's cellular and mitochondrial effects.

Main Methods:

  • Literature review and discussion of existing research on melatonin transport and function.
  • Analysis of the potential impact of GLUT/SLC2A and PEPT1/2 transporters on melatonin's cellular uptake.
  • Comparative analysis of passive diffusion and active transport mechanisms for melatonin.

Main Results:

  • Melatonin is found across diverse organisms, from bacteria to plants and animals.
  • Its functions extend beyond circadian regulation to include antioxidant, neuroprotective, immunomodulatory, and oncostatic effects.
  • Novel transport systems, including GLUT/SLC2A and PEPT1/2, have been identified for melatonin uptake.

Conclusions:

  • Newly identified transporters (GLUT/SLC2A, PEPT1/2) may significantly influence melatonin's cellular actions, especially within mitochondria.
  • Understanding these transport systems is crucial for elucidating melatonin's full range of protective functions.
  • The balance between passive diffusion and active transport dictates melatonin's intracellular distribution and efficacy.