Proteomics

Dataset Information

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DAP5 directs a widespread alternate form of cap-dependent mRNA translation initiation using eIF3d for specialized cell functions


ABSTRACT: Affinity purification of eIF4GII, eIF4GI and DAP5 using a HA tag on the N-terminus of each protein.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Beatrix Ueberheide  

PROVIDER: MSV000082407 | MassIVE | Fri May 25 15:33:00 BST 2018

SECONDARY ACCESSION(S): PXD009923

REPOSITORIES: MassIVE

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Publications

A widespread alternate form of cap-dependent mRNA translation initiation.

de la Parra Columba C   Ernlund Amanda A   Alard Amandine A   Ruggles Kelly K   Ueberheide Beatrix B   Schneider Robert J RJ  

Nature communications 20180803 1


Translation initiation of most mammalian mRNAs is mediated by a 5' cap structure that binds eukaryotic initiation factor 4E (eIF4E). However, inactivation of eIF4E does not impair translation of many capped mRNAs, suggesting an unknown alternate mechanism may exist for cap-dependent but eIF4E-independent translation. We show that DAP5, an eIF4GI homolog that lacks eIF4E binding, utilizes eIF3d to facilitate cap-dependent translation of approximately 20% of mRNAs. Genome-wide transcriptomic and t  ...[more]

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