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Eukaryotic initiation factor (eIF) modulators act on the proteins that start translation of messenger RNA (mRNA). The cap-binding protein eIF4E recruits the scaffold eIF4G and the RNA helicase eIF4A, which together form the eIF4F complex. 4EGI-1, reported in 2007, inhibits the interaction between eIF4E and eIF4G, and 4E1RCat and 4E2RCat disrupt the same assembly. Silvestrol targets eIF4A, while eIF4A3-IN-1 acts on the related helicase eIF4A3. Under cellular stress, phosphorylation of the eIF2α subunit lowers global protein synthesis. Salubrinal, described in 2005, inhibits eIF2α dephosphorylation and protects cells from endoplasmic reticulum (ER) stress. ISRIB (trans-isomer), reported in 2013, restores translation in cells with phosphorylated eIF2α and enhanced memory in rodents.
