Related Experiment Video
Updated: Jun 15, 2026

Measurements of Physiological Stress Responses in C. Elegans
Published on: May 21, 2020
GRP94 in ER quality control and stress responses
Davide Eletto1, Devin Dersh, Yair Argon
1Division of Cell Pathology, Department of Pathology and Lab Medicine, The Children's Hospital of Philadelphia and the University of Pennsylvania, 3615 Civic Center Blvd., Philadelphia, PA 19104, USA.
Glucose Regulated Protein 94 (GRP94) is a key endoplasmic reticulum chaperone. This review details GRP94
Area of Science:
- Cellular Biology
- Molecular Biology
- Protein Folding
Background:
- The endoplasmic reticulum (ER) maintains cellular homeostasis through protein folding.
- Secretory and membrane proteins require chaperones for proper folding.
- Glucose Regulated Protein 94 (GRP94) is a crucial ER chaperone.
Purpose of the Study:
- To review the current understanding of GRP94.
- To elucidate GRP94's multifaceted roles in ER quality control.
Main Methods:
- Literature review of structural and functional data on GRP94.
- Analysis of GRP94's interactions within the ER protein folding machinery.
Main Results:
- GRP94 plays a vital role in chaperoning protein folding.
- It interacts with other ER protein folding components.
- GRP94 contributes to calcium storage within the ER.
- It facilitates the degradation of misfolded proteins via ER-associated degradation (ERAD).
Conclusions:
- GRP94 is essential for ER quality control.
- Its functions include protein folding, interaction with folding machinery, calcium storage, and ERAD.
- Recent data highlight GRP94's unique characteristics and importance.
Related Concept Videos
Protein Folding Quality Check in the RER
The Unfolded Protein Response
Regulation of the Unfolded Protein Response
Other Stress Responses in Bacteria
Export of Misfolded Proteins out of the ER
Stringent Response in E. coli
