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Updated: Jan 21, 2026
16:43
Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
Published on: February 18, 2014
13.6K
Emerging lysosomal pathways for quality control at the endoplasmic reticulum.
Chiara De Leonibus1, Laura Cinque1, Carmine Settembre1,2
1Telethon Institute of Genetics and Medicine (TIGEM), Pozzuoli, Italy.
FEBS Letters
|August 8, 2019
Summary
Misfolded proteins in the endoplasmic reticulum (ER) can cause disease. This review explores ER-to-lysosome-associated degradation pathways, alternative to ER-associated degradation (ERAD), for clearing these proteins.
Area of Science:
- Cellular Biology
- Molecular Biology
- Biochemistry
Background:
- Protein misfolding in the endoplasmic reticulum (ER) is a key factor in many human diseases.
- Cells possess quality control mechanisms to manage misfolded proteins within the ER.
Purpose of the Study:
- To review ERAD-independent mechanisms for clearing misfolded proteins from the ER.
- To highlight alternative pathways like ER-phagy, microautophagy, and vesicular transport.
Main Methods:
- Literature review of existing research on protein quality control in the ER.
- Analysis of ERAD-independent clearance pathways.
Main Results:
- The ER-associated degradation (ERAD) pathway is a primary mechanism for degrading misfolded ER proteins.
- Alternative ERAD-independent pathways, including ER-to-lysosome-associated degradation (ER-phagy, microautophagy, vesicular transport), handle misfolded proteins not cleared by ERAD.
Conclusions:
- Understanding ERAD-independent clearance mechanisms is crucial for developing therapies for protein-aggregation-related disorders.
- Targeting these alternative pathways may offer new therapeutic strategies for diseases linked to protein misfolding.
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