Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Eukaryotic Transcription Inhibitors01:52

Eukaryotic Transcription Inhibitors

11.3K
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...
11.3K
Stringent Response in E. coli01:23

Stringent Response in E. coli

465
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
465
Negative Regulator Molecules01:23

Negative Regulator Molecules

38.9K
Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
38.9K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

15.6K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.6K
Transcription Elongation Factors02:35

Transcription Elongation Factors

14.4K
Transcription elongation is a dynamic process that alters depending upon the sequence heterogeneity of the DNA being transcribed. Hence, it is not surprising that the elongation complex's composition also varies along the way while transcribing a gene.
The transcription elongation is regulated via pausing of RNA polymerase on several occasions during transcription. In bacteria, these halts are necessary because the transcription of DNA into mRNA is coupled to the translation of that mRNA...
14.4K
Phosphorylation01:02

Phosphorylation

55.5K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
55.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

CircZBTB46, a promising therapeutic target in crizotinib resistant ALK-positive T lymphomas.

Leukemia·2026
Same author

Src promotes tumor cell invasion by hijacking the translation machineries.

Cell reports·2026
Same author

CircRNAs derived from the tyrosine phosphatase PTPN22 impact chemosensitivity in ALK-positive T-cell lymphomas.

Scientific reports·2026
Same author

Purinergic signaling promotes gliomagenesis through nuclear calcium transients.

bioRxiv : the preprint server for biology·2026
Same author

Biomarker-Based Eligibility for Lung Cancer Screening: Validation of the Protein-Based INTEGRAL-Risk Model.

JAMA·2026
Same author

Tissue- and tumor-type-specific expression of internal-promoter-driven YEATS-domain-devoid isoforms of MLLT1 and MLLT3.

Biomarker research·2026

Related Experiment Video

Updated: Mar 26, 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

3.4K

4E-BP restrains eIF4E phosphorylation.

David Müller1, Charline Lasfargues1, Sally El Khawand1

  • 1INSERM UMR-1037; Toulouse University; Cancer Research Center of Toulouse (CRCT); Equipe Labellisée Ligue Contre le Cancer and Laboratoire d'Excellence Toulouse Cancer (TOUCAN); Toulouse, France.

Translation (Austin, Tex.)
|January 30, 2016
PubMed
Summary
This summary is machine-generated.

The study reveals how eukaryotic translation initiation factor 4E (eIF4E) phosphorylation is regulated. It shows that 4E-binding protein (4E-BP) plays a key role in controlling eIF4E phosphorylation, independent of MNK kinase expression.

Keywords:
4E-BP14E-BP2MNK1MNK2eIF4EmTORphosphorylation

More Related Videos

Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
10:40

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

Published on: December 28, 2016

8.4K
Xenopus laevis as a Model to Identify Translation Impairment
10:24

Xenopus laevis as a Model to Identify Translation Impairment

Published on: September 27, 2015

11.2K

Related Experiment Videos

Last Updated: Mar 26, 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

3.4K
Analysis of Cap-binding Proteins in Human Cells Exposed to Physiological Oxygen Conditions
10:40

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

Published on: December 28, 2016

8.4K
Xenopus laevis as a Model to Identify Translation Impairment
10:24

Xenopus laevis as a Model to Identify Translation Impairment

Published on: September 27, 2015

11.2K

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Messenger RNA (mRNA) translation in eukaryotes relies on the cap-binding protein eIF4E.
  • eIF4E positions ribosomes at the 5' end of capped mRNA via interactions with the mRNA cap and eIF4G.
  • eIF4E activity is modulated by phosphorylation, catalyzed by the MNK kinase, and this process is influenced by 4E-binding proteins (4E-BPs).

Purpose of the Study:

  • To investigate the regulation of eIF4E phosphorylation.
  • To determine the role of eIF4E-eIF4G interaction and 4E-BP in modulating eIF4E phosphorylation.
  • To elucidate the relationship between mTOR inhibition, 4E-BP, and eIF4E phosphorylation.

Main Methods:

  • Analysis of eIF4E phosphorylation levels under conditions disrupting eIF4E-eIF4G interaction.
  • Assessment of eIF4E phosphorylation following mTOR inhibition and manipulation of 4E-BP levels.
  • Monitoring changes in MNK kinase expression in relation to eIF4E phosphorylation.

Main Results:

  • Disruption of the eIF4E-eIF4G interaction significantly affects eIF4E phosphorylation, irrespective of MNK expression levels.
  • eIF4E phosphorylation is reduced upon eIF4G disruption or sequestration by hypophosphorylated 4E-BP, a consequence of mTOR inhibition.
  • Reducing 4E-BP levels makes eIF4E phosphorylation insensitive to mTOR inhibition.

Conclusions:

  • 4E-binding protein (4E-BP) is crucial for regulating eIF4E phosphorylation.
  • This regulation by 4E-BP occurs independently of changes in MNK kinase expression.
  • The findings highlight a novel regulatory pathway for eIF4E phosphorylation involving 4E-BP and mTOR signaling.