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Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...

Protein Folding Quality Check in the RER

Protein Folding Quality Check in the RER

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...

Export of Misfolded Proteins out of the ER

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...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....

Bacterial Protein Maturation

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

The Unfolded Protein Response

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...

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Related Experiment Video

Updated: Nov 29, 2025

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Fine-tuning ER-phagy by post-translational modifications.

Mohamed A Eldeeb¹, Cornelia E Zorca¹, Mohamed A Ragheb²

¹McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology

|November 19, 2020

Summary

Endoplasmic reticulum autophagy (ER-phagy) selectively degrades the endoplasmic reticulum to maintain cell balance. Recent discoveries reveal new molecular regulators and cross-talk, impacting ER homeostasis and human diseases.

Keywords:

ER-phagy N-degron UFMylation autophagy endoplasmic reticulum lysosome protein degradation proteolysis

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Last Updated: Nov 29, 2025

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

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Published on: February 27, 2020

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Mass Spectrometry Analysis to Identify Ubiquitylation of EYFP-tagged CENP-A EYFP-CENP-A

Published on: June 10, 2020

Area of Science:

Cell Biology
Molecular Biology
Autophagy Research

Background:

Autophagy maintains cellular homeostasis through selective and non-selective pathways.
Endoplasmic reticulum autophagy (ER-phagy) is vital for degrading the endoplasmic reticulum via autophagosomes.
ER-phagy is crucial for organelle homeostasis under physiological and stress conditions.

Purpose of the Study:

To elucidate the molecular regulation of ER-phagy.
To discuss the role of ER-phagy in peripheral endoplasmic reticulum morphology and turnover.
To explore the implications of ER-phagy regulation in human diseases.

Main Methods:

Review of recent literature on ER-phagy.
Analysis of identified ER-phagy receptors and regulators.
Discussion of post-translational modifications and cellular cross-talk in ER-phagy.

Main Results:

Specific receptors targeting ER components for degradation have been identified.
Novel regulators of ER-phagy involving post-translational modifications have been uncovered.
Functional cross-talk between ER-phagy and other cellular processes influences its regulation.

Conclusions:

ER-phagy plays a significant role in managing endoplasmic reticulum morphology and turnover.
Molecular regulation of ER-phagy is complex, involving protein modifications and cellular interactions.
Understanding ER-phagy regulation offers insights into potential therapeutic strategies for related human diseases.