| 2013 |
PPP1R3G functions as a glycogen-targeting subunit (G subunit) of protein phosphatase 1 (PP1) in liver, where it stimulates glycogen synthase activity and promotes hepatic glycogenesis. Liver-specific overexpression increases hepatic glycogen accumulation, accelerates postprandial blood glucose clearance, and reduces hepatic triglyceride levels. The glycogen-binding domain of PPP1R3G is indispensable for its effects on glucose metabolism and triglyceride accumulation. |
Liver-specific transgenic mouse overexpression, primary hepatocyte assays, glycogen synthase activity measurement, domain deletion (glycogen-binding domain mutant) |
Molecular endocrinology (Baltimore, Md.) |
High |
24264575
|
| 2016 |
Whole-body deletion of PPP1R3G reduces glycogen deposition in adipose tissue, decreases fat accumulation, and increases metabolic rate in high-fat diet-fed mice, linking PPP1R3G-mediated glycogen synthesis to lipid metabolism. In 3T3L1 cells, PPP1R3G overexpression increases both glycogen and triglyceride levels. |
Whole-body PPP1R3G knockout mouse model, high-fat diet feeding, metabolic rate measurement (O2/CO2), 3T3L1 cell overexpression assays |
Molecular and cellular endocrinology |
High |
27815211
|
| 2021 |
PPP1R3G recruits its catalytic subunit PP1γ to complex I (TNFR1 signaling complex) to dephosphorylate inhibitory phosphorylation sites on RIPK1 (including serine 25), thereby activating RIPK1 kinase activity and promoting apoptosis and necroptosis. A PPP1R3G mutant that cannot bind PP1γ fails to rescue RIPK1 activation. Ppp1r3g-/- mice are protected from TNF-induced systemic inflammatory response syndrome. |
CRISPR whole-genome knockout screen, PPP1R3G-PP1γ binding mutant rescue experiments, RIPK1 S25A mutation rescue, Ppp1r3g knockout mice with TNF-induced SIRS model |
Nature communications |
High |
34862394
|
| 2023 |
PPP1R3G knockdown in HTR-8/SVneo trophoblasts decreases p-Akt/Akt expression and reduces MMP-9 levels, inhibiting trophoblast migration, invasion, and proliferation via the Akt/MMP-9 signaling pathway. |
Lentiviral knockdown, wound-healing assay, Transwell invasion assay, CCK-8 proliferation assay, western blotting for Akt and MMP-9 pathway components |
Experimental biology and medicine (Maywood, N.J.) |
Medium |
37642261
|
| 2025 |
PPP1R3G deletion in oligodendrocyte precursor cells (OPCs) inhibits OPC differentiation and myelination. Mechanistically, PPP1R3G loss inhibits AMPK, which normally suppresses Drp1 phosphorylation; reduced AMPK activity permits Drp1-mediated mitochondrial fission, disrupting mitochondrial dynamics (reduced length/number, impaired membrane potential and ATP production), thereby impairing OPC differentiation. AMPK activation rescues the fission defects. |
Ppp1r3g KO mice, primary OPC culture, immunohistochemistry, TEM, RNA-seq, mitochondrial functional assays, AMPK activation rescue experiment |
International immunopharmacology |
Medium |
40834529
|
| 2026 |
In doxorubicin-induced cardiotoxicity, DOX triggers p38-mediated inhibitory phosphorylation of RIPK1 as a transient brake. PPP1R3G is recruited to dephosphorylate RIPK1, activating it and triggering early-stage apoptosis. Activated RIPK1 promotes cytosolic release of mitochondrial DNA, inducing ZBP1 expression via IFN-β signaling, which amplifies late-stage necroptosis in a feed-forward loop. Ppp1r3g knockout mice are protected from DOX-induced cardiac dysfunction and mortality. |
Ppp1r3g genetic KO mice, doxorubicin cardiotoxicity model, in vitro cell death assays, cytokine measurement (TNFα, IFN-β, IFN-γ), mtDNA release assay, ZBP1/IFN-β pathway analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
41984837
|