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A Reporter Assay to Analyze Intronic microRNA Maturation in Mammalian Cells

A Reporter Assay to Analyze Intronic microRNA Maturation in Mammalian Cells

Published on: June 16, 2022

Functional characterization of the HuR:CD83 mRNA interaction.

Dorothea Pieper¹, Susann Schirmer, Alexander T Prechtel

¹Department of Cell Biology and Virology, Heinrich Pette Institute - Leibniz Institute for Experimental Virology, Hamburg, Germany.

|August 11, 2011

Summary

The shuttle protein HuR binds CD83 mRNA via its RRM1 and RRM2 domains, facilitating nuclear export. This interaction is crucial for dendritic cell maturation and T-cell activation.

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Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Method for the Isolation and Identification of mRNAs, microRNAs and Protein Components of Ribonucleoprotein Complexes from Cell Extracts using RIP-Chip

Published on: September 29, 2012

Area of Science:

Immunology
Molecular Biology
Cell Biology

Background:

Dendritic cell (DC) maturation involves CD83 expression, essential for T-cell activation.
CD83 mRNA expression is regulated post-transcriptionally by HuR binding to a novel RNA element (PRE).
HuR binding directs CD83 mRNA to the CRM1 nuclear export pathway.

Purpose of the Study:

To investigate the structural basis of the HuR:CD83 mRNA interaction.
To determine the roles of HuR's RNA recognition motifs (RRMs) and the CD83 PRE in binding and export.

Main Methods:

In vitro and in vivo analysis using mutant forms of HuR and CD83 mRNA.
Assessment of protein:RNA complex formation and nuclear export pathways.

Main Results:

HuR's RRM1 and RRM2 domains are critical for binding CD83 mRNA; RRM3 and hinge regions have minor roles.
Specific subfragments within the CD83 PRE are essential for HuR binding.
Disruption of HuR binding redirects CD83 mRNA from CRM1 to the NXF1/TAP export pathway.

Conclusions:

The HuR:CD83 mRNA interaction is structurally defined by specific HuR RRMs and PRE elements.
Functional PRE elements are necessary for CRM1-mediated nuclear export of CD83 mRNA.
Altered HuR binding impacts CD83 mRNA nucleocytoplasmic trafficking, influencing dendritic cell function.