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Casein kinase 1 (CK1)-dependent phosphorylation of rpS6 promotes its association with the mRNA capbinding complex in vitro and protein phosphatase 1 (PP1) antagonizes rpS6 C terminus phosphorylation and cap binding in intact cells (Hutchinson et al.
We have identified a small molecule, guanabenz, which binds to a regulatory subunit of protein phosphatase 1, PPP1R15A/GADD34, selectively disrupting the stress-induced dephosphorylation of the alpha subunit of translation initiation factor 2 (eIF2 alpha).
Protein phosphatase 1 (PP1), a Ser/Thr phosphatase, is the key enzyme responsible for dephosphorylation of lamins in the cell nucleus.