Tyr-94 phosphorylation inhibits pyruvate dehydrogenase phosphatase 1 and promotes tumor growth. [PDF]
Background: How oncogenic signals attenuate mitochondrial function and promote the switch to glycolysis remains unclear. Results: Tyr-94 phosphorylation inhibits mitochondrial PDP1 and is important for the glycolytic switch and tumor growth.
Shan C+14 more
europepmc +4 more sources
Mitochondrial pyruvate dehydrogenase phosphatase 1 regulates the early differentiation of cardiomyocytes from mouse embryonic stem cells. [PDF]
Mitochondria are crucial for maintaining the properties of embryonic stem cells (ESCs) and for regulating their subsequent differentiation into diverse cell lineages, including cardiomyocytes.
Heo HJ+10 more
europepmc +3 more sources
Isoenzymes of Pyruvate Dehydrogenase Phosphatase [PDF]
Pyruvate dehydrogenase phosphatase (PDP) is one of the few mammalian phosphatases residing within the mitochondrial matrix space. It is responsible for dephosphorylation and reactivation of the pyruvate dehydrogenase complex (PDC) and, by this means, is ...
Boli Huang+5 more
semanticscholar +2 more sources
Pyruvate dehydrogenase phosphatase deficiency: identification of the first mutation in two brothers and restoration of activity by protein complementation. [PDF]
CONTEXT Pyruvate dehydrogenase phosphatase (PDP) deficiency has been previously reported as an enzymopathy, but the genetic basis for such a defect has never been established.
M. Maj+7 more
semanticscholar +2 more sources
Cancer cells, when exposed to the hypoxic tumour microenvironment, respond by activating hypoxia‐inducible factors (HIFs). HIF‐1 mediates extensive metabolic re‐programming, and expression of HIF‐1α, its oxygen‐regulated subunit, is associated with poor ...
Angeliki Karagiota+4 more
semanticscholar +2 more sources
Starvation and diabetes reduce the amount of pyruvate dehydrogenase phosphatase in rat heart and kidney. [PDF]
The pyruvate dehydrogenase complex (PDC) is inactivated in many tissues during starvation and diabetes to conserve three-carbon compounds for gluconeogenesis.
Boli Huang+3 more
semanticscholar +2 more sources
Structural Requirements within the Lipoyl Domain for the Ca2+-dependent Binding and Activation of Pyruvate Dehydrogenase Phosphatase Isoform 1 or Its Catalytic Subunit* [PDF]
The inner lipoyl domain (L2) of the dihydrolipoyl acetyltransferase (E2) 60-mer forms a Ca2+-dependent complex with the pyruvate dehydrogenase phosphatase 1 (PDP1) or its catalytic subunit, PDP1c, in facilitating large enhancements of the activities of ...
A. Turkan, X. Gong, T. Peng, T. Roche
semanticscholar +2 more sources
Requirements for the Adaptor Protein Role of Dihydrolipoyl Acetyltransferase in the Up-regulated Function of the Pyruvate Dehydrogenase Kinase and Pyruvate Dehydrogenase Phosphatase* [PDF]
The dihydrolipoyl acetyltransferase (E2 component) is a 60-mer assembled via its COOH-terminal domain with exterior E1-binding domain and two lipoyl domains (L2 then L1) sequentially connected by mobile linker regions.
Daqing Yang+3 more
semanticscholar +2 more sources
Crystallization and preliminary crystallographic studies of the catalytic subunits of human pyruvate dehydrogenase phosphatase isoforms 1 and 2. [PDF]
Pyruvate dehydrogenase phosphatase (PDP) is a mitochondrial serine phosphatase that activates phosphorylated pyruvate dehydrogenase complex by dephosphorylation. In humans, two PDP isoforms (1 and 2) have been identified.
J. Kato, Masato Kato
semanticscholar +2 more sources
Purification of bovine kidney and heart pyruvate dehydrogenase phosphatase on Sepharose derivatized with the pyruvate dehydrogenase complex. [PDF]
Pyruvate dehydrogenase phosphatase has been purified to apparent homogeneity from mitochondrial extracts of both beef heart and beef kidney. An essential step in this three-step purification is affinity chromatography of a largely purified phosphatase ...
M. L. Pratt, J. Maher, T. Roche
semanticscholar +2 more sources