Related Experiment Video
Updated: Aug 6, 2025
10:12
Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity
Published on: June 14, 2024
2.0K
CRELD2, endoplasmic reticulum stress, and human diseases
Qin Tang1, Qinhui Liu1, Yanping Li1
1Department of Pharmacy, Institute of Metabolic Diseases and Pharmacotherapy, West China Hospital, Sichuan University, Chengdu, Sichuan, China.
Frontiers in Endocrinology
|March 20, 2023
Summary
CRELD2, induced by endoplasmic reticulum (ER) stress, is a secreted protein involved in cartilage/bone metabolism. This review explores CRELD2
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- CRELD2 is a secreted protein and ER-resident protein.
- Its expression is induced by ER stress.
- CRELD2 is widely expressed in various tissues.
Purpose of the Study:
- To review the characteristics and functions of CRELD2.
- To explore the role of CRELD2 in human diseases.
- To highlight challenges and future directions for CRELD2 research.
Main Methods:
- Literature review of recent advances in CRELD2 research.
- Summary of ER stress mechanisms.
- Critical analysis of CRELD2's role in various diseases.
Main Results:
- CRELD2 is implicated in cartilage/bone metabolism homeostasis.
- CRELD2 is associated with chronic liver diseases, cardiovascular diseases, kidney diseases, and cancer.
- ER stress significantly influences CRELD2 expression and secretion.
Conclusions:
- CRELD2 plays diverse roles in human health and disease.
- Further research is needed to fully elucidate CRELD2's functions.
- Understanding CRELD2's role in ER stress-related diseases is crucial.
Related Concept Videos
01:17Role of ER in the Secretory Pathway
5.5K
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...
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...
5.5K
01:31Regulation of the Unfolded Protein Response
2.5K
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...
2.5K
01:37The Unfolded Protein Response
4.8K
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...
4.8K
01:32Export of Misfolded Proteins out of the ER
3.7K
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...
3.7K
01:29Protein Folding Quality Check in the RER
3.8K
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...
3.8K
01:21Smooth Endoplasmic Reticulum
5.9K
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...
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...
5.9K