A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
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Updated: Aug 18, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
Published on: May 1, 2020
Maria Alexandra Andrei1, Dierk Ingelfinger, Rainer Heintzmann
1Department of Cellular Biochemistry, Max-Planck-Institute of Biophysical Chemistry, D-37077 Göttingen, Germany.
Abstract:
mRNP remodeling events required for the transition of an mRNA from active translation to degradation are currently poorly understood. We identified protein factors potentially involved in this transition, which are present in mammalian P bodies, cytoplasmic foci enriched in 5' --> 3' mRNA degrading enzymes. We demonstrate that human P bodies contain the cap-binding protein eIF4E and the related factor eIF4E-transporter (eIF4E-T), suggesting novel roles for these proteins in targeting mRNAs for 5' --> 3' degradation. Furthermore, fluorescence resonance energy transfer (FRET) studies indicate that eIF4E interacts with eIF4E-T and the putative DEAD box helicase rck/p54 in the P bodies in vivo. RNAi-mediated knockdowns revealed that a subset of P body factors, including eIF4E-T, LSm1, rck/p54, and Ccr4 are required for the accumulation of each other and eIF4E in P bodies. In addition, treatment of HeLa cells with cycloheximide, which inhibits translation, revealed that mRNA is also required for accumulation of mRNA degradation factors in P bodies. In contrast, knockdown of the decapping enzyme Dcp2, which initiates the actual 5' --> 3' mRNA degradation did not abolish P body formation, indicating it first functions after mRNPs have been targeted to these cytoplasmic foci. These data support a model in which mRNPs undergo several successive steps of remodeling and/or 3' trimming until their composition or structural organization promotes their accumulation in P bodies.
Insights
This study reveals that key proteins like eIF4E and eIF4E-transporter (eIF4E-T) are crucial for mRNA degradation, accumulating in P bodies to target transcripts for decay.
Area of Science:
- Cell Biology
- Molecular Biology
- RNA Biology
Background:
- The transition of messenger RNA (mRNA) from active translation to degradation involves complex remodeling events.
- Protein factors mediating this transition, particularly within mammalian P bodies, are not fully understood.
Purpose of the Study:
- To identify and characterize protein factors involved in mRNA targeting to P bodies for degradation.
- To elucidate the roles of eIF4E and eIF4E-transporter (eIF4E-T) in mRNA decay pathways.
Main Methods:
- Utilized mammalian P bodies as cellular foci for studying mRNA degradation.
- Employed fluorescence resonance energy transfer (FRET) to study protein interactions in vivo.
- Performed RNA interference (RNAi)-mediated knockdowns to assess the requirement of specific factors.
- Used cycloheximide treatment to inhibit translation and study mRNA's role.
Main Results:
- Human P bodies contain eIF4E and eIF4E-T, suggesting their involvement in mRNA targeting for 5' to 3' degradation.
- FRET confirmed interactions between eIF4E, eIF4E-T, and rck/p54 within P bodies.
- Knockdown of eIF4E-T, LSm1, rck/p54, and Ccr4 disrupted the accumulation of these factors and eIF4E in P bodies.
- mRNA presence is necessary for the accumulation of mRNA degradation factors in P bodies.
- Decapping enzyme Dcp2 knockdown did not prevent P body formation, indicating its function post-targeting.
Conclusions:
- mRNP remodeling and P body accumulation are sequential steps in mRNA degradation.
- eIF4E and eIF4E-T play significant roles in targeting mRNAs to P bodies.
- P body formation is dependent on specific degradation factors and mRNA availability, preceding the action of decapping enzymes.
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