Protein phosphatase-1 (PP1) participates in the regulation of a wide variety of cellular functions by reversible protein phosphorylation. The ability of PP1 to regulate diverse functions resides in its capacity to interact with a variety of regulatory subunits that may target PP1 to specific subcellular locations, modulate its substrate specificity, and allow its activity to be responsive to extracellular signals. Several targeting subunits of PP1 have been identified, including PPP1R5, the glycogen-binding subunits GM, GL, PTG and R6 and PPP1R4, and the nuclear inhibitor of PP1 (PPP1R8).[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Doherty MJ, Young PR, Cohen PT (Jan 1997). "Amino acid sequence of a novel protein phosphatase 1 binding protein (R5) which is related to the liver- and muscle-specific glycogen binding subunits of protein phosphatase 1". FEBS Lett. 399 (3): 339–43. doi:10.1016/S0014-5793(96)01357-9. PMID8985175. S2CID31243700.
Armstrong CG, Browne GJ, Cohen P, Cohen PT (1998). "PPP1R6, a novel member of the family of glycogen-targeting subunits of protein phosphatase 1". FEBS Lett. 418 (1–2): 210–4. doi:10.1016/S0014-5793(97)01385-9. PMID9414128. S2CID21169749.