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Related Concept Videos

Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

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...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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 precursors...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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,...
Energy to Drive Translocation01:37

Energy to Drive Translocation

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...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

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Related Experiment Video

Updated: Jun 4, 2026

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

UXT (Ubiquitously Expressed Transcript) causes mitochondrial aggregation.

Tijuana N Moss1, Amy Vo, Wallace L McKeehan

  • 1Center for Cancer and Stem Cell Biology, Institute of Biosciences and Technology, Texas A&M Health Science Center, Texas Medical Center, Houston, TX 77030, USA.

In Vitro Cellular & Developmental Biology. Animal
|June 8, 2007
PubMed
Summary
This summary is machine-generated.

Ubiquitously expressed transcript (UXT) causes mitochondria to aggregate and invade the nucleus, leading to cell death. This study reveals UXT

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Last Updated: Jun 4, 2026

4D Imaging of Protein Aggregation in Live Cells
08:59

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Published on: April 5, 2013

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
11:22

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Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

Published on: May 10, 2022

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitochondria are crucial for cellular energy and apoptosis.
  • Mitochondrial distribution is regulated by the cytoskeleton.
  • Perinuclear mitochondrial aggregation is linked to cell death.

Purpose of the Study:

  • To investigate the role of ubiquitously expressed transcript (UXT) in mitochondrial distribution and cell death.
  • To understand the mechanism by which UXT influences mitochondrial aggregation.

Main Methods:

  • Overexpression of green fluorescent protein-tagged UXT (GFP-UXT) in mammalian cells.
  • Observation of GFP-UXT localization and distribution patterns over time.
  • Correlation of GFP-UXT aggregation with mitochondrial and LRPPRC aggregation.

Main Results:

  • GFP-UXT exhibited four distinct distribution patterns correlating with protein levels and time.
  • UXT overexpression led to progressive mitochondrial aggregation, starting in the cytosol and culminating in nuclear invasion.
  • GFP-UXT aggregates were found to coincide with aggregates of mitochondria and LRPPRC.

Conclusions:

  • Increasing UXT concentrations promote progressive mitochondrial aggregation.
  • UXT may contribute to cell death by associating with LRPPRC, affecting mitochondrial distribution and nuclear integrity.