Stress signals can cause protein kinases, known as EIF-2 kinases, to phosphorylate the α subunit of a protein complex called translation initiation factor 2 (eIF2), resulting in the gene ATF4 being turned on, which will further affect gene expression. eIF2 consists of three subunits: eIF2α, eIF2β and eIF2γ. eIF2α contains two binding sites, one for phosphorylation and one for RNA binding. The kinases work to phosphorylate serine 51 on the α subunit, which is a reversible action. In a cell experiencing normal conditions, eIF2 aids in the initiation of mRNA translation and recognizing the AUG start codon. However, once eIF2α is phosphorylated, the complex’s activity reduces, causing reduction in translation initiation and protein synthesis, while promoting expression of the ATF4 gene.