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Related Concept Videos

Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

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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.
Components of the secretory pathway
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The Unfolded Protein Response01:37

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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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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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Endoplasmic Reticulum01:39

Endoplasmic Reticulum

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The Endoplasmic Reticulum (ER) in eukaryotic cells is a substantial network of interconnected membranes with diverse functions, from calcium storage to biomolecule synthesis. A primary component of the endomembrane system, the ER manufactures phospholipids critical for membrane function throughout the cell. Additionally, the two distinct regions of the ER specialize in the manufacture of specific lipids and proteins.
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The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
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Export of Misfolded Proteins out of the ER01:32

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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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Endoplasmic Reticulum Stress: Implications in Diseases.

Neha Sylvia Walter1, Varun Gorki2, Rishi Bhardwaj3

  • 1Department of Biophysics, Postgraduate Institute of Medical Education and Research (PGIMER), Chandigarh, 160012, India. walterneha@gmail.com.

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This summary is machine-generated.

Endoplasmic reticulum (ER) stress, triggered by unfolded proteins, activates the Unfolded Protein Response (UPR) to restore cell balance. Understanding ER stress pathways is key for developing new disease treatments.

Keywords:
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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The endoplasmic reticulum (ER) is vital for protein synthesis, folding, lipid biosynthesis, and calcium storage.
  • ER dysfunction leads to ER stress, characterized by misfolded proteins and altered cellular redox balance.
  • ER stress initiates the Unfolded Protein Response (UPR) to maintain homeostasis.

Purpose of the Study:

  • To explore the multifaceted roles of the endoplasmic reticulum (ER) in cellular function.
  • To elucidate the mechanisms of ER stress and the Unfolded Protein Response (UPR).
  • To investigate the implications of ER stress in various human diseases and its therapeutic potential.

Main Methods:

  • Review of existing literature on ER function, ER stress, and UPR pathways.
  • Analysis of the molecular sensors (IRE1, PERK, ATF6) involved in UPR.
  • Examination of the link between ER stress and diseases such as neurodegenerative disorders, diabetes, and cancer.

Main Results:

  • ER stress arises from the accumulation of unfolded proteins or disruptions in ER calcium and redox balance.
  • The UPR, mediated by IRE1, PERK, and ATF6, aims to resolve ER stress and restore homeostasis.
  • Severe ER dysfunction can trigger apoptosis.
  • ER stress is implicated in tuberculosis, malaria, Alzheimer's, Parkinson's, diabetes, and cancer.

Conclusions:

  • ER stress plays a critical role in cellular homeostasis and disease pathogenesis.
  • Targeting ER stress pathways offers potential therapeutic strategies for various diseases.
  • Modulating ER stress activation or inhibition can be disease-specific for effective treatment.