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Related Concept Videos

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
Eukaryotic transcription inhibitors usually contain two distinct domains, a DNA...
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...
Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...
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...

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Related Experiment Video

Updated: Jun 19, 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

RhoE inhibits 4E-BP1 phosphorylation and eIF4E function impairing cap-dependent translation.

Priam Villalonga1, Silvia Fernández de Mattos, Anne J Ridley

  • 1Ludwig Institute for Cancer Research, University College London, W1W7BS London, United Kingdom. priam.villalonga@uib.es

The Journal of Biological Chemistry
|October 24, 2009
PubMed
Summary

RhoE, a Rho GTPase, inhibits cell proliferation by blocking the translation of key proteins. It prevents the eukaryotic initiation factor eIF4E from binding to 4E-BP1, thus halting cell cycle progression and transformation.

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Last Updated: Jun 19, 2026

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08:47

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Published on: May 1, 2020

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Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions

Published on: December 28, 2016

Xenopus laevis as a Model to Identify Translation Impairment
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Xenopus laevis as a Model to Identify Translation Impairment

Published on: September 27, 2015

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • RhoE is a Rho GTPase family member known to inhibit RhoA/ROCK signaling.
  • Previous studies indicated RhoE inhibits cell cycle progression and Ras-induced transformation by preventing cyclin D1 translation.

Purpose of the Study:

  • To investigate the molecular mechanisms by which RhoE inhibits cell cycle progression and transformation.
  • To elucidate RhoE's role in regulating protein translation and its impact on cellular proliferation.

Main Methods:

  • Western blotting to assess protein phosphorylation (4E-BP1, S6K) and mTOR/Raptor association.
  • Cell-based assays to evaluate cell cycle progression, Ras-induced transformation, and c-Myc expression/activity.
  • Functional rescue experiments using eIF4E in RhoE-expressing cells.

Main Results:

  • RhoE inhibits 4E-BP1 phosphorylation without affecting mTOR activation.
  • RhoE prevents eIF4E release from 4E-BP1, thereby inhibiting cap-dependent translation.
  • RhoE suppresses c-Myc expression and transcriptional activity, and eIF4E can rescue RhoE-mediated inhibition of proliferation and transformation.

Conclusions:

  • RhoE exerts its anti-proliferative effects by inhibiting eIF4E-mediated cap-dependent translation.
  • The inhibition of eIF4E function is a critical mechanism for RhoE's anti-proliferative and anti-transformation activities.
  • RhoE represents a potential therapeutic target for controlling cell proliferation and oncogenic transformation.