A mechanism of translational repression by competition of Paip2 with eIF4G for poly(A) binding protein (PABP) binding

被引：77

作者：

Karim, Muhammad M.

Svitkin, Yuri V.

Kahvejian, Avak

De Crescenzot, Gregory

Costa-Mattioli, Mauro

Sonenberg, Nahum

机构：

[1] McGill Univ, Dept Biochem, Montreal, PQ H3G 1Y6, Canada

[2] McGill Univ, Ctr Canc, Montreal, PQ H3G 1Y6, Canada

[3] Ecole Polytech Montreal, Dept Chem Engn, Bio Unit P2, Montreal, PQ H3T 1J4, Canada

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2006年 / 103卷 / 25期

关键词：

circularization; translation initiation;

D O I：

10.1073/pnas.0603701103

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The eukaryotic mRNA 3' poly(A) tail and the 5' cap cooperate to synergistically enhance translation. This interaction is mediated by the cap-binding protein eIF4E, the poly(A) binding protein (PABP), and eIF4G, a scaffolding protein that bridges between ORE and PABP to bring about the circularization of the mRNA. The translational repressor, Paip2 (PABP-interacting protein 2), inhibits translation by promoting the dissociation of PABP from poly(A). Here we report on the existence of an alternative mechanism by which Paip2 inhibits translation by competing with eIF4G for binding to PABP. We demonstrate that Paip2 can abrogate the translational activity of PABP, which is tethered to the 3' end of the mRNA. Thus, Paip2 can inhibit translation by a previously unrecognized mechanism, which is independent of its ability to disrupt PABP-poly(A) interaction.

引用

页码：9494 / 9499

页数：6

共 43 条

[1] MESSENGER-RNA POLYADENYLATE-BINDING PROTEIN - GENE ISOLATION AND SEQUENCING AND IDENTIFICATION OF A RIBONUCLEOPROTEIN CONSENSUS SEQUENCE [J].