In order to terminate the integrated stress response, dephosphorylation of eIF2α is required. The protein phosphatase 1 complex (PP1) aids in the dephosphorylation of eIF2α. This complex contains a PP1 catalytic subunit as well as two regulatory subunits. This complex is negatively regulated by two proteins: growth arrest and DNA damage‐inducible protein (GADD34), also known as PPP1R15A, or constitutive repressor of eIF2α phosphorylation (CReP), also known as PPP1R15B. CReP acts to keep levels of eIF2α phosphorylation low in cells under normal conditions. GADD34 is produced in response to ATF4 and works to increase dephosphorylation of eIF2α. The dephosphorylation of eIF2α results in the return of normal protein synthesis and cellular function. However, dephosphorylation of eIF2α can also facilitate the production of death-inducing proteins in cases where the cell is so severely damaged that normal functioning cannot be restored.