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Related Concept Videos

Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

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...
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...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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...
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 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,...

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Related Experiment Video

Updated: Jul 9, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

Endoplasmic reticulum stress in disease pathogenesis.

Jonathan H Lin1, Peter Walter, T S Benedict Yen

  • 1Department of Biochemistry, University of California, San Francisco, CA 94143, USA. Jonathan.Lin@ucsf.edu

Annual Review of Pathology
|November 28, 2007
PubMed
Summary

The unfolded protein response (UPR) is a cellular system that monitors endoplasmic reticulum (ER) protein folding. This review explores UPR

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The endoplasmic reticulum (ER) is crucial for synthesizing and folding proteins in mammalian cells.
  • Proper protein folding is essential for cellular homeostasis and organismal development.
  • Accumulation of misfolded proteins in the ER triggers cellular stress responses.

Purpose of the Study:

  • To provide background information on the unfolded protein response (UPR).
  • To discuss the role of ER stress and UPR in various diseases.
  • To highlight the importance of ER protein quality control.

Main Methods:

  • This review synthesizes existing literature on the unfolded protein response.
  • It examines signaling pathways involved in ER stress.

Related Experiment Videos

Last Updated: Jul 9, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

  • It discusses the link between ER stress and disease pathogenesis.

    • Main Results:

    • The ER has sophisticated signaling pathways to manage misfolded proteins.
    • The unfolded protein response is vital for cellular homeostasis.
    • ER stress is implicated in the development of numerous diseases.

    Conclusions:

    • The unfolded protein response is a critical cellular defense mechanism.
    • Dysregulation of ER homeostasis contributes to disease.
    • Understanding UPR pathways offers therapeutic potential for ER-related disorders.