Phosphorylation effects on the intact structure of eukaryotic translation initiation factor 4B (eIF4B) using ion mobility mass spectrometry

摘要

For the first time, native IMMS shows that eIF4B is present as a dimer and monomer. Neither phosphomimetic nor non-phosphorylated mutants of Ser422 of eIF4B affect the conformation of the eIF4B monomer or dimer. Mutate additional phosphorylation sites of eIF4B to determine their effects on conformation. Determine the role of Ser422 phosphorylation on eIF4B function using biochemical assays examining translation initiation.