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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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ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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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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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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Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

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The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
The recycling endosome is not a single organelle but an extensively tubulated network of recycling pathways. It functions in storing molecules or transporting them across...
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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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Exploring the Regulation of Lipid Droplet Catabolism through Lipophagy
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ER-phagy: Eating the Factory.

Maurizio Molinari1

  • 1Institute for Research in Biomedicine, Faculty of Biomedical Sciences, Università della Svizzera italiana, Bellinzona, Switzerland; School of Life Sciences, École Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.

Molecular Cell
|June 6, 2020
PubMed
Summary

A genome-wide screen identified new mechanisms controlling the degradation of the endoplasmic reticulum during starvation. This research sheds light on cellular adaptation to nutrient deprivation.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Genetics

Background:

  • The endoplasmic reticulum (ER) is a vital organelle involved in protein synthesis and folding.
  • Cellular stress, such as starvation, can lead to ER dysfunction.
  • Understanding the mechanisms of ER degradation is crucial for cellular homeostasis.

Purpose of the Study:

  • To identify novel genes and pathways involved in the starvation-induced degradation of the endoplasmic reticulum.
  • To elucidate the molecular players regulating ER turnover under nutrient deprivation.

Main Methods:

  • Utilized a genome-wide screen in a model organism.
  • Employed techniques to monitor endoplasmic reticulum morphology and degradation.
  • Performed genetic analysis to validate identified genes.

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Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
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Purification of the Membrane Compartment for Endoplasmic Reticulum-associated Degradation of Exogenous Antigens in Cross-presentation
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Main Results:

  • Discovered several previously unknown genes that regulate ER degradation during starvation.
  • Characterized new molecular players contributing to ER turnover in response to nutrient deprivation.
  • Provided insights into the cellular response pathways activated by starvation.

Conclusions:

  • The study reveals novel aspects of endoplasmic reticulum quality control and degradation.
  • Identified key genetic factors influencing cellular adaptation to starvation.
  • Highlights the complex regulatory network governing ER homeostasis under stress.