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metabolic crosstalk is due to decreased mTORC1 and SREBP activity in PTG (show LPCAT3 Proteins) knockout mice or knockdown cells, suggesting a positive feedback loop in which once accumulated, glycogen (show GYS1 Proteins) stimulates the mTORC1/SREBP1 (show SREBF1 Proteins) pathway to shift energy storage to lipogenesis.
removing PTG (show LPCAT3 Proteins), a glycogen (show GYS1 Proteins) synthesis activator protein, nearly completely eliminates Lafora bodies and rescues the neurodegeneration, myoclonus,seizure susceptibility, and behavioral abnormality.
Laforin (show EPM2A Proteins)-deficient mice lacking PTG (show LPCAT3 Proteins) have greatly decreased Lafora bodies and normal glycogen (show GYS1 Proteins) levels.
These data suggest that PTG (show LPCAT3 Proteins) plays a critical role in glycogen (show GYS1 Proteins) synthesis and is necessary to maintain the appropriate metabolic balance for the partitioning of fuel substrates between glycogen (show GYS1 Proteins) and lipid.
PTG (show LPCAT3 Proteins) overexpression in 3T3-L1 adipocytes discretely stimulates PP1 (show PPP1CC Proteins) activity against glycogen synthase and phosphorylase, resulting in a marked and specific increase in glucose uptake and storage as glycogen (show GYS1 Proteins).
These data indicate that disruption of PTG (show LPCAT3 Proteins) expression resulted in the uncoupling of PP1 (show PPP1CC Proteins) activity from glycogen (show GYS1 Proteins) metabolizing enzymes, the enhancement of glycogenolysis, and a dramatic decrease in cellular glycogen (show GYS1 Proteins) levels.
mouse protein targeting to glycogen (PTG) promoter is regulated by the FoxA2 (show FOXA2 Proteins) forkhead protein (show FOXO4 Proteins) and by 3',5'-cyclic adenosine 5'-monophosphate in H4IIE hepatoma cells
PPP1R3C, a novel hypermethylated gene in colorectal cancer, may play a critical role in cancer cell growth in association with glucose levels.
detection of methylation of PPP1R3C alone or in combination with EFHD1 (show EFHD1 Proteins) in plasma DNA showed high sensitivity and specificity in CRC (show CALR Proteins) detection, and may be useful detection method for CRC (show CALR Proteins), especially for early-stage CRCs.
Findings suggest that variations in PTG may condition the course of Lafora disease and establish PTG as a potential target for pharmacogenetic and therapeutic approaches.
Results demonstrated that HIF1 (show HIF1A Proteins) promotes glycogen (show GYS1 Proteins) accumulation through regulating PPP1R3C expression under hypoxia, which revealed a novel metabolic adaptation of cells to hypoxia.
phosphorylation of R5/PTG at Ser (show SIGLEC1 Proteins)-8 by AMPK (show PRKAA1 Proteins) accelerates its laforin (show EPM2A Proteins)/malin (show NHLRC1 Proteins)-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity.
This gene encodes a regulatory subunit of protein phosphatase-1 (PP1). PP1 catalyzes reversible protein phosphorylation, which is important in a wide range of cellular activities: neuronal, muscular, RNA splicing, protein synthesis, cell death, and glycogen metabolism, to name just a few. By interacting with different regulatory subunits, PP1 is directed to different parts of the cell, to different substrates, or to respond to extracellular signals.
PP1 subunit R5
, protein phosphatase 1 binding protein PTG
, protein phosphatase 1 regulatory subunit 3C
, protein phosphatase 1 regulatory subunit 5
, protein phosphatase 1, regulatory (inhibitor) subunit 5
, protein targeting to glicogen
, protein targeting to glycogen
, Phosphatase 1, regulatory inhibitor subunit 5
, protein phosphatase 1, regulatory (inhibitor) subunit 3C