Results 71 to 80 of about 441 (94)

Diacylglycerol kinases

Cellular Signalling, 2004
Diacylglycerol kinases (DGKs) phosphorylate diacylglycerol to form phosphatidic acid. In most cases, members of this large family of enzymes appear to bind and regulate proteins activated by either diacylglycerol or phosphatidic acid. Proteins that appear to be regulated, in part, by DGKs include protein kinase Cs, RasGRPs, and phosphatidylinositol ...
Bai, Luo   +3 more
openaire   +2 more sources

Diacylglycerol kinases in cancer

Advances in Biological Regulation, 2017
Diacylglycerol kinases (DGK) are a family of enzymes that catalyze the transformation of diacylglycerol into phosphatidic acid. In T lymphocytes, DGKα and ζ limit the activation of the PLCγ/Ras/ERK axis, providing a critical checkpoint to inhibit T cell responses. Upregulation of these isoforms limits Ras activation, leading to hypo-responsive, anergic
Isabel Mérida   +7 more
openaire   +2 more sources

Diacylglycerol Kinase

2009
Diacylglycerol kinase (DGK, EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). DGK belongs to a well-conserved family of proteins found in diverse species, such as Saccharomyces cerevisiae, Drosophila melanogaster, Caenorhabditis elegans, mammals, plants, and bacteria (Merida et al.
Arisz, S.A., Munnik, T.
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Properties and functions of diacylglycerol kinases

Cellular Signalling, 2000
Diacylglycerol kinases (DGKs) phosphorylate the second-messenger diacylglycerol (DAG) to phosphatidic acid (PA). The family of DGKs is well conserved among most species. Nine mammalian isotypes have been identified, and are classified into five subgroups based on their primary structure.
W J, van Blitterswijk, B, Houssa
openaire   +2 more sources

Diacylglycerol kinases in signal transduction

Chemistry and Physics of Lipids, 1999
Diacylglycerol kinase (DGK) phosphorylates the second messenger diacylglycerol (DAG) to phosphatidic acid. A family of nine mammalian isotypes have been identified. Their primary structure shows a diverse array of conserved domains, such as a catalytic domain, zinc fingers, pleckstrin homology domains and EF-hand structures, known to interact with ...
W J, van Blitterswijk, B, Houssa
openaire   +2 more sources

An endogenous regulator of diacylglycerol kinase

Biochemical and Biophysical Research Communications, 1988
During the initial steps of the subcellular fractionation of rat brain homogenate, we recovered more than 100% of diacylglycerol kinase activity. The unusually high yields prompted us to examine the possibility that we had removed an endogenous inhibitor from diacylglycerol kinase during those steps.
I M, Jeng, N, Klemm, C Z, Wu
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Diacylglycerol kinase control of protein kinase C

Biochemical Journal, 2019
Abstract The diacylglycerol kinases (DGK) are lipid kinases that transform diacylglycerol (DAG) into phosphatidic acid (PA) in a reaction that terminates DAG-based signals. DGK provide negative regulation to conventional and novel protein kinase C (PKC) enzymes, limiting local DAG availability in a tissue- and subcellular-restricted ...
Isabel Mérida   +3 more
openaire   +3 more sources

Diacylglycerol kinase

1996
Abstract Diacylglycerol kinase (DGK) reverses the normal flow of phospholipid biosynthesis by phosphory/ating diacylglycerol back to phosphatidic acid. DGK consists of a number of isozymes with different enzymological properties. The three isozymes so far sequenced, however, share highly conserved regions including two sets each of EF-
openaire   +1 more source

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