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Related Concept Videos

Autophagy01:27

Autophagy

6.1K
Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
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Autophagic Cell Death01:18

Autophagic Cell Death

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Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and...
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Delivery Pathways to the Lysosome01:36

Delivery Pathways to the Lysosome

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Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
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Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

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Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
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The Unfolded Protein Response01:37

The Unfolded Protein Response

7.0K
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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Related Experiment Video

Updated: Apr 3, 2026

Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry
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Assessing Autophagic Flux by Measuring LC3, p62, and LAMP1 Co-localization Using Multispectral Imaging Flow Cytometry

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ER Stress and Autophagy.

W-S Lee, W-H Yoo, H-J Chae1

  • 1Department of Pharmacology and Institute of Cardiovascular Research, School of Medicine, Chonbuk National University, Jeonju 561-180, South Korea. hjchae@jbnu.ac.kr.

Current Molecular Medicine
|September 23, 2015
PubMed
Summary

Endoplasmic reticulum (ER) stress triggers the unfolded protein response (UPR) to manage cellular damage. If unresolved, ER stress activates autophagy, a self-degradative process with therapeutic potential.

Area of Science:

  • Cellular biology
  • Molecular biology
  • Stress response pathways

Background:

  • Eukaryotic cells encounter stress from environmental changes and internal factors like misfolded proteins.
  • Accumulation of misfolded proteins in the endoplasmic reticulum (ER) activates the unfolded protein response (UPR).
  • The UPR initiates a recovery process involving chaperones and other proteins.

Purpose of the Study:

  • To review the intricate relationship between ER stress and autophagy.
  • To explore the adaptive and potentially detrimental roles of the UPR.
  • To highlight the therapeutic implications of targeting the ER stress-autophagy nexus.

Main Methods:

  • Literature review of cellular stress responses.
  • Analysis of the unfolded protein response (UPR) pathways.

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Related Experiment Videos

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Study of Protein-protein Interactions in Autophagy Research
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  • Investigation into the role of autophagy in cellular homeostasis.
  • Main Results:

    • ER stress, if excessive or prolonged, can lead to cell death via apoptosis.
    • ER stress is a significant inducer of autophagy, a self-degradative cellular process.
    • Autophagy plays an adaptive role in managing ER stress.

    Conclusions:

    • The interplay between ER stress and autophagy is crucial for cellular survival and adaptation.
    • Understanding this intersection offers potential avenues for therapeutic intervention in various diseases.
    • Targeting the ER stress-autophagy pathway may provide novel treatment strategies.