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Related Concept Videos

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
The Unfolded Protein Response01:37

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...
Transcriptional Regulation: Riboswitches01:23

Transcriptional Regulation: Riboswitches

Riboswitches are RNA elements that regulate gene expression by altering their secondary structures in response to specific effector molecules. These elements, located in the leader regions of certain mRNAs, act as transcriptional regulators by toggling between alternative conformations to control downstream gene expression. Riboswitch-mediated regulation is a precise mechanism for modulating biosynthetic pathways, as exemplified by the riboflavin biosynthesis pathway in Bacillus...
Translational Regulation01:29

Translational Regulation

Translational regulation in prokaryotes ensures efficient protein synthesis by controlling ribosome access to mRNA. This regulation is mediated by secondary RNA structures, including translational riboswitches, RNA thermometers, and small RNAs (sRNAs), which respond to intracellular and environmental signals to modulate gene expression.Translational RiboswitchesRiboswitches in the leader region of mRNAs can regulate translation by altering the accessibility of the Shine-Dalgarno (SD) sequence,...
Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...

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Related Experiment Video

Updated: May 19, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

Published on: June 14, 2024

Stress-Responsive Protein IFRD1 Protects Assembled Ribosomes via a Ribosome-Salvaging Mechanism.

Charles J Cho1,2,3, Molly K Crowder4, Amala K Rougeau4

  • 1Division of Digestive Diseases, Department of Medicine, Emory University, Atlanta, GA.

Biorxiv : the Preprint Server for Biology
|May 18, 2026
PubMed
Summary
This summary is machine-generated.

IFRD1 protein stabilizes ribosomes during cellular stress and regeneration. Its absence leads to ribosome degradation, impaired mTORC1 activity, and increased cell death, crucial for understanding paligenosis.

Keywords:
IFRD1injurypaligenosisribosomesalvaging

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Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using &#967;CRAC
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Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

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Last Updated: May 19, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
10:12

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication

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Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using &#967;CRAC
09:15

Monitoring Protein-RNA Interaction Dynamics In Vivo at High Temporal Resolution Using χCRAC

Published on: May 9, 2020

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Regenerative Medicine

Background:

  • Epithelial cell regeneration relies on coordinated responses to injury.
  • IFRD1 (Iron-regulated gene 1) is a stress-responsive protein essential for paligenosis (cellular regeneration).
  • The precise mechanism of IFRD1 in paligenosis remains unclear.

Purpose of the Study:

  • To elucidate the molecular function of IFRD1 in cellular regeneration and stress response.
  • To investigate the role of IFRD1 in ribosome stability and cellular homeostasis.

Main Methods:

  • In vivo and in vitro injury models (cerulein-induced pancreatitis, tunicamycin-induced ER stress).
  • Biochemical assays to identify IFRD1 binding partners (ribosomes).
  • Analysis of ribosome stability, autophagic flux, p62 accumulation, and mTORC1 activity.

Main Results:

  • IFRD1 binds to non-translating 80S monosomes in the cytosol.
  • IFRD1 functions as a ribosome-salvaging factor, preventing ribosome degradation during ER stress.
  • Loss of IFRD1 leads to ribosome instability, p62 accumulation, reduced mTORC1 activity, and increased cell death.

Conclusions:

  • IFRD1 plays a critical role in preserving the mature ribosome pool during cellular stress and transitions like paligenosis.
  • IFRD1's function in ribosome stabilization is a previously unrecognized cellular mechanism.
  • Understanding IFRD1's role is key to comprehending cellular regeneration and stress response pathways.