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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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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
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Reduced Expression of Oligodendrocyte Linage-Enriched Transcripts During the Endoplasmic Reticulum Stress/Integrated

Yonglin Gao1,2, Lukasz P Slomnicki1,2, Ewa Kilanczyk1,2

  • 1Kentucky Spinal Cord Injury Research Center, University of Louisville School of Medicine, Louisville, Kentucky, USA.

ASN Neuro
|July 18, 2024
PubMed
Summary
This summary is machine-generated.

Endoplasmic reticulum (ER) stress disrupts oligodendrocyte (OL) gene expression, impacting cell proliferation and identity. This molecular disruption is observed in various central nervous system (CNS) diseases, potentially leading to myelin damage.

Keywords:
Differentiationendoplasmic reticulum stressintegrated stress responsemyelinationoligodendrocyte precursor cellstranscriptomewhite matter injury

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Endoplasmic reticulum (ER) stress in oligodendrocyte (OL) lineage cells is implicated in central nervous system (CNS) pathologies like spinal cord injury (SCI) and multiple sclerosis.
  • Understanding the transcriptomic changes in OLs under ER stress is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the transcriptomic alterations in OL precursor cells (OPCs) induced by ER stress.
  • To determine the impact of ER stress on OL-specific gene expression and cell proliferation.

Main Methods:

  • Primary rat OPCs were treated with ER stress-inducing agents thapsigargin (TG) or tunicamycin (TM).
  • RNA sequencing (RNASeq) was performed to analyze global gene expression changes.
  • Gene Ontology (GO) enrichment analysis was used to identify affected biological pathways.

Main Results:

  • Both TG and TM upregulated general stress response genes.
  • Tunicamycin (TM) selectively enriched ER stress-related gene ontology terms.
  • ER stress downregulated cell cycle/proliferation transcripts and key OL lineage-enriched genes, including Olig2.
  • Similar downregulation of OL-specific genes was observed in mature OLs from mouse models of CNS white matter pathologies.

Conclusions:

  • ER stress significantly disrupts the transcriptomic profile of OL lineage cells.
  • This disruption affects OL identity and proliferation, potentially contributing to myelin degeneration and dysfunction in CNS diseases.
  • The findings highlight ER stress as a critical factor in OL pathology across various neurological conditions.