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Related Experiment Video

Updated: Jun 13, 2026

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

Published on: January 24, 2016

A 3'UTR polymorphism disrupts IRF2BP2 autoregulation through an eIF4H translational enhancer.

An Duong^1,2,3, Hsiao-Huei Chen^3,4,5,6, Alexandre F R Stewart^1,2,3

¹Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, Canada.

Frontiers in Genetics

|June 12, 2026

Summary

A genetic variant in IRF2BP2 (Interferon regulatory factor 2 binding protein 2) disrupts translation, lowering protein levels and increasing heart disease risk. This variant affects how IRF2BP2 regulates itself, impacting inflammation and atherosclerosis.

Keywords:

eukaryotic translation initiation factor 4H genetic polymorphism interferon regulatory factor (IRF)macrophage translation regulation

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Last Updated: Jun 13, 2026

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

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Published on: January 24, 2016

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

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Published on: May 1, 2020

Xenopus laevis as a Model to Identify Translation Impairment

Xenopus laevis as a Model to Identify Translation Impairment

Published on: September 27, 2015

Area of Science:

Molecular Biology
Genetics
Immunology

Background:

Interferon regulatory factor 2 binding protein 2 (IRF2BP2) plays a role in suppressing interferon responses and inflammation.
A specific 9-nucleotide deletion in the 3'UTR of IRF2BP2 (rs3045215) is associated with reduced protein expression and increased risk of coronary atherosclerosis and calcification.

Purpose of the Study:

To investigate the molecular mechanism by which the IRF2BP2 3'UTR deletion variant affects protein expression and translation.
To elucidate the role of eukaryotic initiation factor 4H (eIF4H) in IRF2BP2 autoregulation.

Main Methods:

RNAfold analysis to predict RNA structures.
siRNA knockdown of eIF4H.
Luciferase reporter assays with wild-type and deletion-variant IRF2BP2 3'UTRs.
RNA gel mobility shift assays using macrophage extracts.

Main Results:

The 9-nucleotide deletion disrupts an RNA stem-loop structure necessary for eIF4H recruitment and translation enhancement.
siRNA knockdown of eIF4H reduced endogenous IRF2BP2 protein levels and impaired reporter gene translation.
The deletion variant prevented IRF2BP2 protein from interacting with its own 3'UTR RNA.

Conclusions:

The rs3045215 deletion variant abolishes IRF2BP2 autoregulation by disrupting an eIF4H-dependent translational enhancer.
This mechanism contributes to lower IRF2BP2 protein levels and increased cardiovascular disease risk.