Poly(A)-binding protein-interacting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation.

Abstract:

:Poly(A)-binding protein (PABP) stimulates translation initiation by binding simultaneously to the mRNA poly(A) tail and eukaryotic translation initiation factor 4G (eIF4G). PABP activity is regulated by PABP-interacting (Paip) proteins. Paip1 binds PABP and stimulates translation by an unknown mechanism. Here, we describe the interaction between Paip1 and eIF3, which is direct, RNA independent, and mediated via the eIF3g (p44) subunit. Stimulation of translation by Paip1 in vivo was decreased upon deletion of the N-terminal sequence containing the eIF3-binding domain and upon silencing of PABP or several eIF3 subunits. We also show the formation of ternary complexes composed of Paip1-PABP-eIF4G and Paip1-eIF3-eIF4G. Taken together, these data demonstrate that the eIF3-Paip1 interaction promotes translation. We propose that eIF3-Paip1 stabilizes the interaction between PABP and eIF4G, which brings about the circularization of the mRNA.

journal_name

Mol Cell Biol

authors

Martineau Y,Derry MC,Wang X,Yanagiya A,Berlanga JJ,Shyu AB,Imataka H,Gehring K,Sonenberg N

doi

10.1128/MCB.00738-08

subject

Has Abstract

pub_date

2008-11-01 00:00:00

pages

6658-67

issue

21

eissn

0270-7306

issn

1098-5549

pii

MCB.00738-08

journal_volume

28

pub_type

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