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Related Concept Videos

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

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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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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.
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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A heuristic is a general problem-solving framework (Tversky & Kahneman, 1974). You can think of these as mental shortcuts that are used to solve problems. Different types of heuristics are used in different types of situations, and the impulse to use a heuristic occurs when one of five conditions is met (Pratkanis, 1989):
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Psychology is the scientific discipline dedicated to understanding both observable behavior and the internal mental processes underlying such behavior. It aims to comprehend human nature and apply this understanding to solve practical problems, enhance well-being, and improve societal outcomes. An example of psychology's application is the study of prosocial behavior, such as why and under what conditions individuals might help strangers in need. This process involves describing observed...
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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Inadequate BiP availability defines endoplasmic reticulum stress.

Milena Vitale1, Anush Bakunts1, Andrea Orsi1,2

  • 1Division of Genetics and Cell Biology, San Raffaele Scientific Institute, Milan, Italy.

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|March 15, 2019
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Summary

Endoplasmic reticulum (ER) stress causes cell damage when the chaperone BiP is insufficient. The unfolded protein response (UPR) and ER-associated degradation (ERAD) pathways protect cells by restoring proteostasis.

Keywords:
BiP/GRP78ER stresscell biologychaperonesendoplasmic reticulumhumanproteotoxicityunfolded protein response

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Endoplasmic reticulum (ER) stress and its link to cytotoxicity remain unclear.
  • Previous work demonstrated HeLa cells can restore homeostasis during proteostatic ER stress via the unfolded protein response (UPR).

Purpose of the Study:

  • To elucidate the mechanisms by which ER stress leads to cytotoxicity.
  • To define the role of BiP chaperone availability in ER proteotoxicity.

Main Methods:

  • Inducible bulk expression of secretory immunoglobulin M heavy chain (µs) in HeLa cells.
  • Investigating the impact of abrogating ER-associated degradation (ERAD) and specific UPR pathways (ATF6α).
  • Analyzing the effect of removing the BiP-sequestering CH1 domain from µs.

Main Results:

  • Conditions preventing BiP restoration over µs lead to µs-driven proteotoxicity.
  • Abrogation of HRD1-mediated ERAD or the ATF6α UPR branch results in proteotoxicity.
  • Removal of the CH1 domain from µs allows tolerance under these conditions.

Conclusions:

  • Proteostatic ER stress is a consequence of inadequate BiP availability.
  • The UPR and ERAD pathways are crucial for mitigating BiP-deficiency-induced proteotoxicity.
  • BiP availability is a critical determinant of cellular response to ER stress.