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Related Concept Videos

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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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 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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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
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
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The Unfolded Protein Response01:37

The Unfolded Protein Response

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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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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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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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Related Experiment Video

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Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
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Endoplasmic reticulum proteostasis impairment in aging.

Gabriela Martínez1,2,3,4, Claudia Duran-Aniotz1,2,3, Felipe Cabral-Miranda1,2,3,5

  • 1Center for Geroscience, Brain Health and Metabolism, Santiago, Chile.

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Neuronal proteostasis decline contributes to brain aging and neurodegenerative diseases. Enhancing the unfolded protein response (UPR) may offer therapeutic strategies against pathological brain aging.

Keywords:
agingendoplasmic reticulumendoplasmic reticulum stressprotein misfolding disordersunfolded protein response

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Aging Research

Background:

  • Perturbed neuronal proteostasis is common in aging and protein misfolding disorders.
  • The proteostasis network maintains proteome health through synthesis, folding, trafficking, secretion, and degradation pathways.
  • Reduced proteostasis buffering during aging increases neurodegeneration risk via misfolded protein accumulation.

Purpose of the Study:

  • To review evidence linking endoplasmic reticulum (ER) stress to brain aging.
  • To explore the role of the neuronal unfolded protein response (UPR) in organismal proteostasis.
  • To discuss therapeutic interventions for improving proteostasis and preventing pathological brain aging.

Main Methods:

  • Literature review of recent evidence on ER stress, UPR, and brain aging.
  • Analysis of the impact of neuronal UPR on global proteostasis.
  • Discussion of potential therapeutic strategies.

Main Results:

  • ER stress is identified as a driver of brain aging.
  • Neuronal UPR plays a crucial role in maintaining ER homeostasis and influencing organismal proteostasis.
  • Misfolded protein accumulation is linked to reduced proteostasis capacity in aging.

Conclusions:

  • ER stress is a key factor in brain aging and neurodegeneration.
  • Targeting neuronal UPR presents a potential therapeutic avenue for age-related brain dysfunction.
  • Maintaining proteostasis is critical for preventing pathological brain aging.