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Protein Folding Quality Check in the RER

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Related Experiment Video

Updated: Jun 12, 2026

4D Imaging of Protein Aggregation in Live Cells

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Sorting things out through endoplasmic reticulum quality control.

Taku Tamura¹, Johan C Sunryd, Daniel N Hebert

¹Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA.

Molecular Membrane Biology

|June 18, 2010

Summary

This summary is machine-generated.

The endoplasmic reticulum (ER) quality control machinery identifies and processes misfolded proteins. Proteins are either corrected or degraded via the ER-associated degradation (ERAD) pathway.

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Assays for the Degradation of Misfolded Proteins in Cells

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

The endoplasmic reticulum (ER) is a critical organelle for protein synthesis and maturation within the eukaryotic secretory pathway.
Protein folding is an intricate process prone to errors, leading to misfolded proteins and aggregates.
Cellular integrity necessitates mechanisms to manage and eliminate aberrant proteins.

Purpose of the Study:

To elucidate the components and mechanisms of the ER's protein quality control (PQC) system.
To understand how the ER distinguishes between native and non-native proteins.
To detail the cellular fate of misfolded proteins, including rescue and degradation pathways.

Main Methods:

The abstract does not specify methods but implies a review or synthesis of recent findings.
Focuses on the identification of machinery involved in ER quality control.
Examines the mechanisms governing protein evaluation, retention, and degradation.

Main Results:

Proteins are rigorously evaluated within the ER for proper folding and maturation.
Native proteins are sorted for transport, while misfolded proteins are retained for potential correction.
Terminally misfolded proteins are targeted for degradation through the ER-associated degradation (ERAD) pathway.

Conclusions:

The ER possesses sophisticated quality control mechanisms to maintain proteostasis.
The ERAD pathway is essential for removing terminally misfolded proteins, preventing cellular damage.
Recent advances have significantly improved our understanding of ER quality control machinery and its function.