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Related Concept Videos

Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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,...
Regulation of Expression at Multiple Steps01:23

Regulation of Expression at Multiple Steps

The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the addition of a...
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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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Related Experiment Video

Updated: May 20, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

Translational homeostasis via eIF4E and 4E-BP1.

Alan G Hinnebusch1

  • 1Laboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. ahinnebusch@nih.gov

Molecular Cell
|July 4, 2012
PubMed
Summary

The translational repressor 4E-BP1 regulates protein synthesis by targeting its partner eIF4E for degradation. This mechanism ensures translation continues even when eIF4E levels are low.

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Last Updated: May 20, 2026

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Area of Science:

  • Molecular biology
  • Cellular regulation
  • Protein synthesis

Background:

  • The eukaryotic initiation factor 4E (eIF4E) is a key regulator of cap-dependent translation.
  • 4E-binding proteins (4E-BPs) inhibit eIF4E activity, thereby repressing translation.
  • The precise control of 4E-BP1 abundance and its interaction with eIF4E is crucial for cellular homeostasis.

Discussion:

  • Yanagiya et al. reveal a novel regulatory loop connecting 4E-BP1 levels to eIF4E availability.
  • Proteasomal degradation of 4E-BP1 is shown to be a critical step in this feedback mechanism.
  • This degradation process allows for the maintenance of translation under conditions of eIF4E limitation.

Key Insights:

  • A regulatory mechanism couples 4E-BP1 abundance with its target eIF4E.
  • Proteasomal degradation of 4E-BP1 is central to this coupling.
  • This pathway ensures translation persists in cells with reduced eIF4E levels.

Outlook:

  • Further investigation into the upstream signals controlling 4E-BP1 proteasomal degradation.
  • Exploring the therapeutic potential of modulating this pathway in diseases associated with translation dysregulation.
  • Understanding the broader implications of this regulatory mechanism in cellular stress responses.