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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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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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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

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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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Protein quality control in the endoplasmic reticulum.

Paul-Albert Koenig1, Hidde L Ploegh2

  • 1Klinikum rechts der Isar, Technische Universität München, Institut für Klinische Chemie und Pathobiochemie, Ismaninger Straße 22, 81675 München Germany.

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Summary

Biological membranes allow protein transport, crucial for cellular needs. This review focuses on removing unwanted proteins from the endoplasmic reticulum (ER) in whole animals, not just cell cultures.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Biological membranes, including the endoplasmic reticulum (ER), regulate the passage of molecules.
  • Specialized transport and translocation mechanisms exist for moving substances across these barriers.
  • Protein homeostasis is vital for cellular function and overall organismal health.

Purpose of the Study:

  • To review mechanisms for removing unwanted proteins from the endoplasmic reticulum (ER).
  • To highlight the importance of studying these processes in whole animals, beyond traditional cell culture models.
  • To emphasize the need for tailored solutions to protein quality control in diverse cell types and tissues.

Main Methods:

  • Literature review of protein removal pathways from the ER.
  • Analysis of existing studies on protein translocation and degradation.
  • Comparative assessment of findings from cell culture versus whole animal models.

Main Results:

  • Membrane barriers are selectively permeable, facilitating controlled protein movement.
  • The ER plays a critical role in managing protein synthesis and degradation.
  • Cellular and tissue-specific variations necessitate adaptable protein quality control strategies.

Conclusions:

  • Understanding ER protein removal is essential for maintaining cellular homeostasis.
  • Extrapolation of findings from simple models to complex organisms requires careful consideration.
  • Tailored approaches are needed to manage protein turnover across different biological contexts.