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Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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,...
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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,...
Endoplasmic Reticulum01:39

Endoplasmic Reticulum

Endoplasmic ReticulumThe endoplasmic reticulum (ER) is an extensive network of membranous sacs and tubules in eukaryotic cells, continuous with the outer membrane of the nucleus. This structural continuity integrates nuclear and cytoplasmic processes and facilitates efficient intracellular transport. This allows mRNA to move directly from the nucleus to ribosomes for efficient protein synthesis. As a result, the ER serves as a central site for the synthesis, processing, and distribution of...
The Unfolded Protein Response01:37

The Unfolded Protein Response

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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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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Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells
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Published on: December 17, 2012

Quality and quantity control at the endoplasmic reticulum.

Ramanujan S Hegde1, Hidde L Ploegh

  • 1Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. hegder@mail.nih.gov

Current Opinion in Cell Biology
|June 24, 2010
PubMed
Summary
This summary is machine-generated.

Cells control protein quality and quantity within the endoplasmic reticulum (ER), the organelle responsible for maturing one-third of cellular proteins. This review synthesizes pathways for protein degradation from the ER under normal and disease conditions.

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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The endoplasmic reticulum (ER) is crucial for synthesizing and maturing secretory and membrane proteins.
  • These proteins constitute approximately one-third of the cellular proteome.
  • Cellular homeostasis relies on strict regulation of protein synthesis and quality control within the ER.

Purpose of the Study:

  • To synthesize current understanding of protein degradation pathways originating from the ER.
  • To discuss the role and regulation of ER-associated degradation (ERAD) under physiological and pathological conditions.

Main Methods:

  • Literature review and synthesis of existing research on ER protein degradation.
  • Analysis of pathways involved in targeting misfolded or excess proteins for degradation.
  • Examination of the implications of ER protein homeostasis in disease.

Main Results:

  • Detailed overview of the mechanisms governing protein removal from the ER.
  • Identification of key components and regulatory steps in ER-associated degradation (ERAD).
  • Exploration of how dysregulation of these pathways contributes to various pathologies.

Conclusions:

  • ER protein degradation pathways are essential for maintaining cellular health.
  • Understanding ERAD is critical for developing therapeutic strategies for diseases linked to protein misfolding.
  • Continued research into ER protein homeostasis promises insights into fundamental cell biology and disease mechanisms.