Poly(A)-Binding Protein-Interacting Protein 1 Binds to Eukaryotic Translation Initiation Factor 3 To Stimulate Translation

被引：104

作者：

Martineau, Yvan ^{[1
]}

Derry, Melanie C. ^{[1
]}

Wang, Xiaoshan ^{[1
]}

Yanagiya, Akiko ^{[1
]}

Berlanga, Juan Jose ^{[3
]}

Shyu, Ann-Bin ^{[4
]}

Imataka, Hiroaki ^{[5
]}

Gehring, Kalle ^{[1
]}

Sonenberg, Nahum ^{[1
,2
]}

机构：

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

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

[3] Univ Autonoma Madrid, Fac Ciencias, Ctr Biol Mol Severo Ochoa, E-28049 Madrid, Spain

[4] Univ Texas Houston, Sch Med, Dept Biochem & Mol Biol, Houston, TX 77030 USA

[5] RIKEN, Syst & Struct Biol Ctr, Tsurumi Ku, Yokohama, Kanagawa, Japan

来源：

MOLECULAR AND CELLULAR BIOLOGY | 2008年 / 28卷 / 21期

基金：

美国国家卫生研究院; 加拿大健康研究院;

关键词：

D O I：

10.1128/MCB.00738-08

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：6658 / 6667

页数：10

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