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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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Regulation of the Unfolded Protein Response01:31

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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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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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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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Chromatin Structure Regulates pre-mRNA Processing02:41

Chromatin Structure Regulates pre-mRNA Processing

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In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...
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Alternative RNA Splicing02:18

Alternative RNA Splicing

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Alternative RNA splicing is the regulated splicing of exons and introns to produce different mature mRNAs from a single pre-mRNA. Unlike in constitutive splicing where a single gene produces a single type of mRNA, alternative splicing allows an organism to produce multiple proteins from a single gene and plays an important role in protein diversity.
There are five types of alternative RNA splicing that vary in the ways the pre-mRNA segments are removed or retained in the mature mRNA. The first...
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Related Experiment Video

Updated: May 30, 2025

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Splicing factor PRP-19 regulates mitochondrial stress response.

Peixue Xia1,2, Liankui Zhou1,2, Jialiang Guan3

  • 1State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China.

Life Metabolism
|January 28, 2025
PubMed
Summary

Splicing factors like PRP-19 are crucial for the mitochondrial unfolded protein response (UPRmt) in animals. This discovery reveals a conserved pathway linking mitochondrial health, immunity, and longevity.

Keywords:
lifespanmitochondriasplicingstress responseunfolded protein response

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Area of Science:

  • Cellular Biology
  • Genetics
  • Aging Research

Background:

  • Mitochondrial perturbation triggers the mitochondrial unfolded protein response (UPRmt) to maintain cellular homeostasis.
  • UPRmt activation in *C. elegans* is linked to innate immunity and extended lifespan.

Purpose of the Study:

  • To investigate the role of splicing factors in the UPRmt pathway.
  • To determine if splicing factors influence UPRmt-mediated immune response and lifespan extension.

Main Methods:

  • Utilized *Caenorhabditis elegans* as a model organism.
  • Investigated the function of splicing factor Precursor RNA processing 19 (PRP-19).
  • Performed knockdown experiments in mammalian cells to assess conserved mechanisms.

Main Results:

  • Splicing factor PRP-19 is essential for UPRmt induction in *C. elegans*.
  • PRP-19 modulates the innate immune response and lifespan extension triggered by mitochondrial stress.
  • PRP-19 knockdown in mammalian cells impairs UPRmt activation and mitochondrial network integrity.

Conclusions:

  • Splicing factors play a critical, evolutionarily conserved role in maintaining mitochondrial homeostasis.
  • PRP-19 links mitochondrial health to innate immunity and organismal lifespan.
  • This study uncovers a novel mechanism regulating mitochondrial function and stress response.