Eukaryotic translation initiation factor 2 alpha phosphatase

Eukaryotic translation initiation factor 2 alpha phosphatase is a cellular enzyme complex that specifically removes phosphate groups from the α subunit of eukaryotic translation initiation factor 2 (eIF2α) after it has been phosphorylated in response to stress. This dephosphorylation step is a critical regulatory event for resuming general protein synthesis following stress recovery. The phosphatase complex consists of protein phosphatase 1 (PP1) as the catalytic core and specific regulatory subunits (primarily GADD34 or CReP in mammals) that confer substrate specificity toward eIF2α. It plays an essential role in controlling the integrated stress response (ISR) by regulating the switch between attenuation and reactivation of global mRNA translation and is implicated in diseases related to stress adaptation, including cancer, neurodegeneration, and infections. Pharmacological inhibitors targeting eIF2α phosphatase are under investigation as potential therapeutics in diseases with dysregulated ISR signaling[2][1].

Other names

eIF2α phosphataseeIF2α-specific phosphatasePPP1R15A/PPP1R15B complexes (when referring to regulatory subunits)GADD34-containing protein phosphatase 1 complexCReP-containing protein phosphatase 1 complex

Inhibition of eIF2α phosphatase increases eIF2α phosphorylation and sustains stress responses, reducing protein synthesis Release of eIF2α phosphatase inhibition restores normal protein synthesis rates after cellular stress