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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
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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Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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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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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Smooth Endoplasmic Reticulum01:21

Smooth Endoplasmic Reticulum

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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.
The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
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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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Endoplasmic Reticulum Stress and Related Pathological Processes.

Yu Mei1, Melissa D Thompson1, Richard A Cohen1

  • 1Vascular Biology Section, Boston University School of Medicine, Boston, Massachusetts 02118, USA.

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|March 11, 2014
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Endoplasmic reticulum (ER) stress, triggered by various cellular insults, involves key sensors like IRE-1, PERK, and ATF6. Understanding ER stress interactions with inflammation and metabolism is crucial for disease control.

Keywords:
ApoptosisAutophagyCalciumER stressHypoxiaInflammationLipidsMitochondrial dysfunction

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Pathology

Background:

  • The endoplasmic reticulum (ER) is vital for protein and lipid synthesis and calcium regulation.
  • ER stress is a cellular response to various insults, including hypoxia and nutrient deprivation.
  • Key sensors mediating the ER stress response include IRE-1, PERK, and ATF6.

Purpose of the Study:

  • To review the intricate relationship between ER stress and pathological processes.
  • To explore the role of ER stress in inflammation, apoptosis, autophagy, and mitochondrial dysfunction.
  • To present the correlation of ER stress with lipid and calcium homeostasis in disease development.

Main Methods:

  • Literature review of ER stress mechanisms and pathological implications.
  • Analysis of the interplay between ER stress sensors and cellular functions.
  • Synthesis of current knowledge on ER stress in disease.

Main Results:

  • ER stress is implicated in inflammation, apoptosis, aberrant autophagy, and mitochondrial dysfunction.
  • Dysregulation of lipid and calcium homeostasis is closely linked to ER stress.
  • ER stress contributes significantly to the development of various diseases.

Conclusions:

  • A deeper understanding of ER stress and its cofactors offers new insights into disease pathogenesis.
  • Targeting ER stress pathways may provide novel therapeutic strategies for disease control.
  • ER stress is a central player in maintaining cellular homeostasis and its disruption leads to pathology.