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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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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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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 Membranes01:45

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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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Mitochondrial Membranes01:45

Mitochondrial Membranes

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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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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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Related Experiment Video

Updated: Mar 17, 2026

Chemical Inactivation of the E3 Ubiquitin Ligase Cereblon by Pomalidomide-based Homo-PROTACs
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Mitochondrial cereblon functions as a Lon-type protease.

Kosuke Kataoka1, China Nakamura1, Toru Asahi1,2

  • 1Faculty of Science and Engineering, Waseda University, TWIns, 2-2 Wakamatsu, Shinjuku, Tokyo 162-8480, Japan.

Scientific Reports
|July 16, 2016
PubMed
Summary

Cereblon (CRBN) partially localizes to mitochondria and exhibits Lon protease activity, protecting neuronal cells from oxidative stress. This suggests CRBN functions as a mitochondrial Lon-type protease.

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Area of Science:

  • Mitochondrial biology
  • Protease function
  • Neuroprotection

Background:

  • Mitochondrial Lon protease is crucial for protein quality control, degrading damaged proteins and protecting cells from oxidative stress.
  • Cereblon (CRBN), linked to intellectual disability, possesses a conserved Lon domain, but its protease function is unknown.
  • Investigating CRBN's role in mitochondria and its potential protective functions against cellular stress is essential.

Purpose of the Study:

  • To determine if Cereblon (CRBN) possesses Lon protease-like function within mitochondria.
  • To evaluate CRBN's protective role against oxidative stress in neuronal cells.
  • To elucidate the specific mitochondrial function of CRBN.

Main Methods:

  • Mitochondrial expression of CRBN in human neuroblastoma SH-SY5Y cells.
  • Assessment of mitochondrial functions including fusion, fission, and membrane potential.
  • Analysis of CRBN protease activity under oxidative stress conditions.
  • Evaluation of neuronal cell death suppression induced by hydrogen peroxide.

Main Results:

  • Mitochondrially expressed CRBN demonstrated protease activity, which was upregulated by oxidative stress.
  • CRBN partially localized to mitochondria, indicating a role in this organelle.
  • Stable SH-SY5Y cell lines expressing mitochondrial CRBN showed reduced neuronal cell death following hydrogen peroxide exposure.
  • No significant impact on mitochondrial fusion, fission, or membrane potential was observed.

Conclusions:

  • Cereblon (CRBN) functions as a Lon-type protease within the mitochondria.
  • CRBN contributes to cellular protection against oxidative stress, specifically in neuronal cells.
  • This finding reveals a novel role for CRBN in mitochondrial protein quality control and neuroprotection.