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 Bioljournal_title
Molecular and cellular biologyauthors
Martineau Y,Derry MC,Wang X,Yanagiya A,Berlanga JJ,Shyu AB,Imataka H,Gehring K,Sonenberg Ndoi
10.1128/MCB.00738-08subject
Has Abstractpub_date
2008-11-01 00:00:00pages
6658-67issue
21eissn
0270-7306issn
1098-5549pii
MCB.00738-08journal_volume
28pub_type
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