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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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In the present study, the expression is knocked down of two downstream signaling components of the PERK pathway, the cytoprotective calcineurin and the pro-apoptotic CHOP, by using specific shRNAs. In opposite ways, these modulate the susceptibility of primary cortical neurons to neurite atrophy after induction of endoplasmic reticulum stress.
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We describe the imaging approaches we use to investigate the distribution and mobility of the transfected fluorescent proteins resident in the endoplasmic reticulum (ER) by means of the confocal imaging of living cells. We also ultrastructurally analyze the effect of their expression on the architecture of this subcellular...
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Smooth Endoplasmic Reticulum01:21

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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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Here we describe a method to visualize endoplasmic reticulum-associated mRNAs in mammalian tissue culture cells. This technique involves the selective permeabilization of the plasma membrane with digitonin to remove cytoplasmic contents followed by fluorescent in situ hybridization to detect either bulk poly(A) mRNA or specific...
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Endoplasmic Reticulum : RER and SER
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Information processing by endoplasmic reticulum stress sensors.

Wylie Stroberg1, Justin Eilertsen1, Santiago Schnell1,2

  • 1Department of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, MI, USA.

Journal of the Royal Society, Interface
|September 12, 2019
PubMed
Summary

The unfolded protein response (UPR) sensor gains more information about endoplasmic reticulum (ER) stress by using both unfolded proteins and chaperones. This dual regulation refines ER stress measurements, explaining its evolutionary advantage.

Keywords:
chemical sensingendoplasmic reticulum stressmutual informationsignal integrationunfolded protein response

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Area of Science:

  • Cellular biology
  • Molecular biology
  • Biophysics

Background:

  • The unfolded protein response (UPR) maintains protein folding homeostasis in the endoplasmic reticulum (ER).
  • ER stress triggers UPR via sensors in the ER membrane, which are regulated by chaperones and unfolded proteins.
  • The functional advantage of this bidirectional sensor control remains unclear.

Purpose of the Study:

  • To investigate the benefit of combined chaperone and unfolded protein regulation of UPR sensors.
  • To determine how this dual regulation impacts the accuracy of ER stress measurement.
  • To provide a rationale for the evolution of this sensing mechanism.

Main Methods:

  • Computational modeling of UPR sensor dynamics.
  • Analysis of information transfer in biological signaling pathways.
  • Mathematical modeling of sensor response to varying protein folding loads.

Main Results:

  • Combining positive regulation by unfolded proteins and negative regulation by chaperones enhances sensor information capacity.
  • This bidirectional control broadens the sensor's active range, improving ER stress measurement.
  • Increased information capacity comes at the cost of higher uncertainty due to multi-signal integration.

Conclusions:

  • Bidirectional regulation of UPR sensors provides a more informative measurement of ER stress.
  • This mechanism optimizes cellular response to proteotoxic stress.
  • The findings offer a potential evolutionary explanation for the observed UPR sensor control.