ArticleThe Biochemical journal1989
Phosphorylation of diacylglycerol kinase in vitro by protein kinase C.
Article in The Biochemical journal, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 53 citations in OpenAlex.
- Diacylglycerol kinase α is a critical signaling node and novel therapeutic target in glioblastoma and other cancers.Cancer discovery · 2013Article
- Bacterial expression strategies for several Sus scrofa diacylglycerol kinase alpha constructs: solubility challenges.Scientific reports · 2013Article
- Fatty acids inhibit growth-factor-induced diacylglycerol kinase alpha activation in vascular smooth-muscle cells.The Biochemical journal · 2001Article
- Purification and characterization of sn-1-stearoyl-2-arachidonoylglycerol kinase from pig testes.The Biochemical journal · 1997Article
- Cloning and expression of a cytoskeleton-associated diacylglycerol kinase that is dominantly expressed in cerebellum.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Membrane-associated diacylglycerol kinase activity is increased by noradrenaline, but not by angiotensin II, in arterial smooth muscle.The Biochemical journal · 1994Article
- Phosphorylation and redistribution of the phosphatidylinositol-transfer protein in phorbol 12-myristate 13-acetate- and bombesin-stimulated Swiss mouse 3T3 fibroblasts.The Biochemical journal · 1993Article
- Diacylglycerol kinase is phosphorylated in vivo upon stimulation of the epidermal growth factor receptor and serine/threonine kinases, including protein kinase C-epsilon.The Biochemical journal · 1993Article
- Cytosolic rat brain synapsin I is a diacylglycerol kinase.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We investigated the effects of enzyme phosphorylation in vitro on the properties of diacylglycerol kinase. Diacylglycerol kinase and protein kinase C, both present as Mr-80,000 proteins, were highly purified from pig thymus cytosol. Protein kinase C phosphorylated diacylglycerol kinase (up to 1 mol of 32P/mol of enzyme) much more actively than did cyclic AMP-dependent protein kinase. Phosphorylated and non-phosphorylated diacylglycerol kinase showed a similar pI, approx. 6.8. Diacylglycerol kinase phosphorylated by either protein kinase C or cyclic AMP-dependent protein kinase was almost exclusively associated with phosphatidylserine membranes. In contrast, soluble kinase consisted of the non-phosphorylated form. The catalytic properties of the lipid kinase were not much affected by phosphorylation, although phosphorylation-linked binding with phosphatidylserine vesicles resulted in stabilization of the enzyme activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.