Protein phosphatase 1 regulatory subunit 3D (PPP1R3D)

Protein phosphatase 1 regulatory subunit 3D (PPP1R3D) is a regulatory protein that acts as a glycogen-targeting subunit for protein phosphatase 1 (PP1), one of the major serine/threonine-specific protein phosphatases in eukaryotic cells[2][3][4][5]. PPP1R3D recruits PP1 to glycogen particles and modulates its substrate specificity, facilitating dephosphorylation of enzymes critical for glycogen synthesis and breakdown, such as glycogen synthase (GS) and glycogen phosphorylase (GP)[2][4]. It contains a conserved RVXF motif for PP1 binding, a separate motif for interacting with glycogenic substrates, and another binding site for 14-3-3 proteins, which regulate its stability and activity[2][4][6]. PPP1R3D plays important roles in glycogen homeostasis, cell division, protein synthesis, and muscle contractility[3][5]. Mutations or dysfunction of PPP1R3D have been linked to certain forms of epilepsy and may contribute to metabolic or neurological disease[3]. No drugs currently target PPP1R3D directly, and its modulation primarily influences PP1 activity and glycogen metabolism.

Other names

PPP1R3DPPP1R6PP1 subunit R6Protein phosphatase 1 regulatory subunit 6Protein phosphatase 1-binding subunit R6Spinophilin

Drugs targeting PP1 or related pathways (such as kinase/phosphatase modulators) would indirectly impact PPP1R3D function by altering PP1 recruitment or activity, but no known drugs directly target PPP1R3D