General RNA-binding Proteins Have a Function in Poly(A)-binding Protein-dependent Translation

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 2008 Dec 17

PMID 19078965

Citations 40

Authors

Yuri V Svitkin

Valentina M Evdokimova

Ann Brasey

Tatyana V Pestova

Daniel Fantus

Akiko Yanagiya

Hiroaki Imataka

Maxim A Skabkin

Lev P Ovchinnikov

William C Merrick

Nahum Sonenberg

Affiliations

Soon will be listed here.

Abstract

The interaction between the poly(A)-binding protein (PABP) and eukaryotic translational initiation factor 4G (eIF4G), which brings about circularization of the mRNA, stimulates translation. General RNA-binding proteins affect translation, but their role in mRNA circularization has not been studied before. Here, we demonstrate that the major mRNA ribonucleoprotein YB-1 has a pivotal function in the regulation of eIF4F activity by PABP. In cell extracts, the addition of YB-1 exacerbated the inhibition of 80S ribosome initiation complex formation by PABP depletion. Rabbit reticulocyte lysate in which PABP weakly stimulates translation is rendered PABP-dependent after the addition of YB-1. In this system, eIF4E binding to the cap structure is inhibited by YB-1 and stimulated by a nonspecific RNA. Significantly, adding PABP back to the depleted lysate stimulated eIF4E binding to the cap structure more potently if this binding had been downregulated by YB-1. Conversely, adding nonspecific RNA abrogated PABP stimulation of eIF4E binding. These data strongly suggest that competition between YB-1 and eIF4G for mRNA binding is required for efficient stimulation of eIF4F activity by PABP.

Citing Articles

Yeast poly(A)-binding protein (Pab1) controls translation initiation in vivo primarily by blocking mRNA decapping and decay.

Poonia P, Valabhoju V, Li T, Iben J, Niu X, Lin Z Nucleic Acids Res. 2025; 53(5).

PMID: 40071937 PMC: 11897895. DOI: 10.1093/nar/gkaf143.

Yeast poly(A)-binding protein (Pab1) controls translation initiation in vivo primarily by blocking mRNA decapping and decay.

Poonia P, Valabhoju V, Li T, Iben J, Niu X, Lin Z bioRxiv. 2024; .

PMID: 38903079 PMC: 11188147. DOI: 10.1101/2024.04.19.590253.

Increased levels of eIF2A inhibit translation by sequestering 40S ribosomal subunits.

Grove D, Levine D, Kearse M Nucleic Acids Res. 2023; 51(18):9983-10000.

PMID: 37602404 PMC: 10570035. DOI: 10.1093/nar/gkad683.

mRNA- and factor-driven dynamic variability controls eIF4F-cap recognition for translation initiation.

Cetin B, OLeary S Nucleic Acids Res. 2022; 50(14):8240-8261.

PMID: 35871304 PMC: 9371892. DOI: 10.1093/nar/gkac631.

PABP prevents the untimely decay of select mRNA populations in human cells.

Kajjo S, Sharma S, Chen S, Brothers W, Cott M, Hasaj B EMBO J. 2022; 41(6):e108650.

PMID: 35156721 PMC: 8922270. DOI: 10.15252/embj.2021108650.

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