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 Experiment Videos

Ebp1 is a dsRNA-binding protein associated with ribosomes that modulates eIF2alpha phosphorylation.

Massimo Squatrito1, Monica Mancino, Leonardo Sala

  • 1European Institute of Oncology, 435 Via Ripamonti, 20141 Milan, Italy. massimo.squatrito@ifom-ieo-campus.it

Biochemical and Biophysical Research Communications
|April 25, 2006
PubMed
Summary

Ebp1 is a novel dsRNA-binding protein that inhibits eIF2alpha phosphorylation, a key step in controlling protein translation. This discovery suggests Ebp1

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

The ARTEMIS trial identifies immune activation as a key predictor of neoadjuvant chemotherapy response in triple-negative breast cancer.

Breast cancer research : BCR·2026
Same author

Effectiveness on Frailty of an eHealth-Based Rehabilitation Program in Older People with Acute Heart Failure and/or Acute Coronary Syndrome: Study Protocol for a Randomized Trial and Baseline Data of Participants.

Journal of clinical medicine·2026
Same author

Author Correction: Oncogene ablation-resistant pancreatic cancer cells depend on mitochondrial function.

Nature·2026
Same author

DPY30 Is an Epigenetic Decoupler Linking Replication Stress to Immunoediting in Pancreatic Cancer.

Cancer research·2026
Same author

Syndecan-1-targeted therapeutic antibody impairs macropinocytosis and elicits antitumor immunity in pancreatic cancer.

Cell reports. Medicine·2026
Same author

p53 Is a Master Regulator of Proteostasis in SMARCB1-Deficient Malignant Rhabdoid Tumors.

Cancer cell·2026

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • dsRNA-binding domains (dsRBDs) are crucial for various cellular processes, including RNA processing and translational control.
  • Eukaryotic initiation factor 2 alpha (eIF2alpha) phosphorylation, triggered by cellular stress, leads to a shutdown of protein translation.
  • Ebp1 is a known regulator of cell growth and a component of ribonucleoprotein (RNP) complexes.

Purpose of the Study:

  • To investigate the role of Ebp1 in RNA binding and its functional implications.
  • To determine if Ebp1's dsRBD mediates dsRNA interactions and affects its cellular localization and RNP complex formation.
  • To explore Ebp1's function in regulating eIF2alpha phosphorylation and protein translation.

Main Methods:

  • Protein domain analysis to identify dsRBD in Ebp1.

Related Experiment Videos

  • Deletion mutagenesis to assess the role of Ebp1's dsRBD.
  • Immunofluorescence microscopy to track Ebp1 localization.
  • Co-immunoprecipitation assays to study protein interactions.
  • Western blotting to analyze eIF2alpha phosphorylation levels.

    • Main Results:

    • Ebp1 possesses a functional dsRBD that mediates its binding to dsRNA.
    • Deletion of the dsRBD disrupts Ebp1's nucleolar localization and RNP complex formation.
    • Ebp1 associates with cytoplasmic ribosomes and inhibits eIF2alpha phosphorylation.
    • Ebp1 overexpression protects eIF2alpha from phosphorylation, even under stress conditions.
    • Ebp1 interacts with and is phosphorylated by PKR.

    Conclusions:

    • Ebp1 is identified as a novel dsRNA-binding protein.
    • Ebp1's dsRBD is essential for its localization and RNP complex formation.
    • Ebp1 acts as a cellular inhibitor of eIF2alpha phosphorylation, suggesting a role in translational control.