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

机译:Poly(A)结合蛋白相互作用蛋白1与真核翻译起始因子3结合以刺激翻译。

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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.
机译:聚(A)结合蛋白(PABP)通过同时与mRNA聚(A)尾巴和真核翻译起始因子4G(eIF4G)结合来刺激翻译起始。 PABP活性受PABP相互作用(Paip)蛋白调节。 Paip1结合PABP并通过未知机制刺激翻译。在这里,我们描述Paip1和eIF3之间的相互作用,这是直接的,独立于RNA并通过eIF3g(p44)亚基介导。当缺失包含eIF3结合域的N端序列以及PABP或几个eIF3亚基沉默后,Paip1在体内对翻译的刺激作用就会降低。我们还显示了由Paip1-PABP-eIF4G和Paip1-eIF3-eIF4G组成的三元复合物的形成。综上所述,这些数据表明eIF3-Paip1相互作用促进翻译。我们建议eIF3-Paip1稳定PABP和eIF4G之间的相互作用,从而引起mRNA的环化。

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