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Related Concept Videos

Redox Reactions01:27

Redox Reactions

1.2K
Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
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Redox Reactions01:24

Redox Reactions

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Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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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...
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Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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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...
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Redox Equilibria: Overview01:23

Redox Equilibria: Overview

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A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

4.3K
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...
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Related Experiment Video

Updated: Apr 26, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Redox regulation in the endoplasmic reticulum.

Neil J Bulleid1, Marcel van Lith1

  • 1*Institute of Molecular, Cellular and Systems Biology, College of Medical Veterinary and Life Sciences, Davidson Building, University of Glasgow, Glasgow G12 8QQ, U.K.

Biochemical Society Transactions
|August 12, 2014
PubMed
Summary

Maintaining the endoplasmic reticulum

Area of Science:

  • Cellular biology
  • Protein folding
  • Biochemistry

Background:

  • Protein secretion is vital for mammalian cell function.
  • Disulfide bond formation is crucial for protein folding and stability.
  • Endoplasmic reticulum redox balance is essential for correct disulfide formation.

Purpose of the Study:

  • To review mechanisms for maintaining endoplasmic reticulum redox balance.
  • To explore pathways that introduce reducing equivalents into the endoplasmic reticulum.
  • To propose methods for testing hypotheses on reductive pathways.

Main Methods:

  • Literature review of endoplasmic reticulum redox homeostasis.
  • Analysis of known oxidizing pathways.
  • Discussion of potential reductive mechanisms and experimental approaches.

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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

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Last Updated: Apr 26, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Assessment of Cellular Oxidation using a Subcellular Compartment-Specific Redox-Sensitive Green Fluorescent Protein
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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Main Results:

  • Current understanding of endoplasmic reticulum oxidation is more advanced than reduction.
  • Potential mechanisms for introducing reducing equivalents are not well-defined.
  • A framework for experimental testing of reductive pathways is proposed.

Conclusions:

  • The precise mechanisms for endoplasmic reticulum reductive balance remain elusive.
  • Further research is needed to elucidate counterbalancing reductive pathways.
  • Investigating these pathways is critical for understanding protein folding diseases.