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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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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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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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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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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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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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A Phenotyping Regimen for Genetically Modified Mice Used to Study Genes Implicated in Human Diseases of Aging
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ER-phagy and human diseases.

Christian A Hübner1, Ivan Dikic2,3,4

  • 1Institute of Human Genetics, University Hospital Jena, Friedrich-Schiller-Universität Jena, Jena, Germany. Christian.Huebner@med.uni-jena.de.

Cell Death and Differentiation
|October 30, 2019
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Summary
This summary is machine-generated.

Autophagy receptors control cellular component degradation. This update focuses on endoplasmic reticulum-phagy (ER-phagy) receptors, crucial for maintaining cellular health and disease prevention.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Autophagy is a fundamental cellular process for degrading damaged or unnecessary components.
  • Autophagosome formation is key to autophagy, engulfing cellular material for lysosomal degradation.
  • Autophagy receptors, defined by LC3-interaction regions (LIRs) or GABARAP-interaction motifs (GIMs), ensure substrate specificity.

Purpose of the Study:

  • To provide an updated overview of endoplasmic reticulum-phagy (ER-phagy) receptors.
  • To highlight the role of ER-phagy receptors in cellular homeostasis and disease pathogenesis.
  • To consolidate current knowledge on the mechanisms and functions of ER-phagy.

Main Methods:

  • Literature review of recent studies on ER-phagy.
  • Analysis of identified ER-phagy receptors and their interaction motifs (LIR/GIM).
  • Synthesis of data on the involvement of ER-phagy in various physiological and pathological contexts.

Main Results:

  • Several receptors mediating ER degradation via autophagy (ER-phagy) have been recently identified.
  • These receptors utilize LIR or GIM motifs to interact with the autophagy machinery.
  • ER-phagy plays a significant role in maintaining endoplasmic reticulum quality control.

Conclusions:

  • ER-phagy receptors are critical regulators of cellular homeostasis.
  • Dysregulation of ER-phagy contributes to the development of various diseases.
  • Further research into ER-phagy receptors holds therapeutic potential for disease management.