DAP5 associates with eIF2β and eIF4AI to promote Internal Ribosome Entry Site driven translation | Zendy

Noa Liberman | Zendy; Valentina Gandin | Zendy; Yuri V. Svitkin | Zendy; Maya David | Zendy; Geneviève Virgili | Zendy; Maritza Jaramillo | Zendy; Martin Holčı́k | Zendy; Bhushan Nagar | Zendy; Adi Kimchi | Zendy; Nahum Sonenberg | Zendy

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DAP5 associates with eIF2β and eIF4AI to promote Internal Ribosome Entry Site driven translation

Author(s) -

Noa Liberman,

Valentina Gandin,

Yuri V. Svitkin,

Maya David,

Geneviève Virgili,

Maritza Jaramillo,

Martin Holčı́k,

Bhushan Nagar,

Adi Kimchi,

Nahum Sonenberg

Publication year - 2015

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gkv205

Subject(s) - internal ribosome entry site , eif4g , eif4e , biology , translation (biology) , eukaryotic translation initiation factor 4 gamma , eukaryotic translation , initiation factor , five prime untranslated region , microbiology and biotechnology , ribosomal binding site , eukaryotic initiation factor , translational regulation , ribosome , messenger rna , genetics , rna , gene

Initiation is a highly regulated rate-limiting step of mRNA translation. During cap-dependent translation, the cap-binding protein eIF4E recruits the mRNA to the ribosome. Specific elements in the 5'UTR of some mRNAs referred to as Internal Ribosome Entry Sites (IRESes) allow direct association of the mRNA with the ribosome without the requirement for eIF4E. Cap-independent initiation permits translation of a subset of cellular and viral mRNAs under conditions wherein cap-dependent translation is inhibited, such as stress, mitosis and viral infection. DAP5 is an eIF4G homolog that has been proposed to regulate both cap-dependent and cap-independent translation. Herein, we demonstrate that DAP5 associates with eIF2β and eIF4AI to stimulate IRES-dependent translation of cellular mRNAs. In contrast, DAP5 is dispensable for cap-dependent translation. These findings provide the first mechanistic insights into the function of DAP5 as a selective regulator of cap-independent translation.

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