Neddylation of phosphoenolpyruvate carboxykinase 1 controls glucose metabolism.
Summary Neddylation is a post-translational mechanism that adds a ubiquitin-like protein, namely neural precursor cell expressed developmentally downregulated protein 8 (NEDD8). Here, we show that neddylation in mouse liver is modulated by nutrient availability.
Gonzalez-Rellan MJ+27 more
europepmc +7 more sources
T3 and glucose increase expression of phosphoenolpyruvate carboxykinase (PCK1) leading to increased β-cell proliferation [PDF]
Objectives: Thyroid hormone (T3) and high glucose concentrations are critical components of β-cell maturation and function. In the present study, we asked whether T3 and glucose signaling pathways coordinately regulate transcription of genes important ...
Liora S. Katz+3 more
doaj +2 more sources
Phosphoenolpyruvate carboxykinases as emerging targets in cancer therapy
Metabolic reprogramming is commonly accompanied by alterations in the expression of metabolic enzymes. These metabolic enzymes not only catalyze the intracellular metabolic reaction, but also participate in a series of molecular events to regulate tumor ...
Yong Yu, Jingying Li, Kaiming Ren
doaj +3 more sources
Characterization of interaction and ubiquitination of phosphoenolpyruvate carboxykinase by E3 ligase UBR5 [PDF]
Phosphoenolpyruvate carboxykinase (PEPCK1) is ubiquitinated by E3 ubiquitin ligase UBR5, which was thought to be facilitated by the acetylation of Lys70, Lys71 and Lys594 in PEPCK1.
Qingya Shen+4 more
doaj +2 more sources
Succinate Dehydrogenase-Regulated Phosphoenolpyruvate Carboxykinase Sustains Copulation Fitness in Aging C. elegans Males [PDF]
Summary: Dysregulated metabolism accelerates reduced decision-making and locomotor ability during aging. To identify mechanisms for delaying behavioral decline, we investigated how C.
Jimmy Goncalves+7 more
doaj +2 more sources
Association of mitochondrial phosphoenolpyruvate carboxykinase with prognosis and immune regulation in hepatocellular carcinoma [PDF]
Mitochondrial phosphoenolpyruvate carboxykinase (PCK2), a mitochondrial isoenzyme, supports the growth of cancer cells under glucose deficiency conditions in vitro.
Chenxuan Li+5 more
doaj +2 more sources
Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis. [PDF]
Tuberculosis, the second leading infectious disease killer after HIV, remains a top public health priority. The causative agent of tuberculosis, Mycobacterium tuberculosis (Mtb), which can cause both acute and clinically latent infections, reprograms ...
Iva Machová+9 more
doaj +2 more sources
O-GlcNAcylation mediates the control of cytosolic phosphoenolpyruvate carboxykinase activity via Pgc1α. [PDF]
PGC1α is a coactivator of many transcription factors and cytosolic phosphoenolpyruvate carboxykinase (PCK1) is a key enzyme for gluconeogenesis. PGC1α interacts with the transcription factor PPARγ to stimulate PCK1 expression and thus de novo glucose ...
Pedro Latorre+4 more
doaj +2 more sources
Protective effect of phosphoenolpyruvate carboxykinase 1 on inflammation and fibrotic progression of IgA nephropathy [PDF]
Introduction Phosphoenolpyruvate carboxykinase 1 (PCK1) is an essential enzyme of the gluconeogenic pathway, which can affect kidney physiology in various ways.
Ya-yin Tan+6 more
doaj +2 more sources
The phosphoenolpyruvate carboxykinase (PEPCK) inhibitor, 3-mercaptopicolinic acid (3-MPA), induces myogenic differentiation in C2C12 cells [PDF]
Phosphoenolpyruvate carboxykinase (PEPCK) is a gluconeogenic enzyme with a cytosolic (Pck1/PEPCK-C) and mitochondrial (Pck2/PEPCK-M) isoform. Here we investigate the effect of 3-mercaptopicolinic acid (3-MPA), a PEPCK inhibitor, on C2C12 muscle cells. We
Madelaine C. Brearley+4 more
doaj +2 more sources