BIOMAT Database Logo BIOMAT Database Logo

Diacylglycerol kinase is phosphorylated in vivo upon stimulation of the epidermal growth factor receptor and serine/threonine kinases, including protein kinase C-epsilon. 1993

D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
Division of Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam.

In signal transduction, diacylglycerol (DG) kinase attenuates levels of the second messenger DG by converting it to phosphatidic acid. A previously cloned full-length human 86 kDa DG kinase cDNA was expressed as fusion protein in Escherichia coli, to aid in the generation of DG-kinase-specific monoclonal antibodies suitable for immunoprecipitation experiments. To investigate whether phosphorylation of DG kinase is a possible mechanism for its regulation, COS-7 cells were transiently transfected with the DG kinase cDNA and phosphorylation of the expressed DG kinase was induced by various stimuli. Activation of both cyclic AMP-dependent protein kinase and protein kinase C (PKC) resulted in phosphorylation of DG kinase on serine residues in vivo, and both kinases induced this phosphorylation within the same tryptic phosphopeptide, suggesting that they may exert similar control over DG kinase. No phosphorylation was observed upon ionomycin treatment, intended to activate Ca2+/calmodulin-dependent kinases. Co-transfections of DG kinase with either PKC-alpha or PKC-epsilon cDNA revealed that both protein kinases, when stimulated, are able to phosphorylate DG kinase. For PKC-epsilon, DG kinase is the first in vivo substrate identified. Stimulation with epidermal growth factor (EGF) of COS-7 cells transfected with both DG kinase and EGF-receptor cDNA results mainly in phosphorylation of DG kinase on tyrosine. Since the EGF receptor has an intrinsic tyrosine kinase activity, this finding implies that DG kinase may be a direct substrate for the activated EGF receptor.

UI MeSH Term Description Entries
D010449 Peptide Mapping Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases. Fingerprints, Peptide,Peptide Fingerprinting,Protein Fingerprinting,Fingerprints, Protein,Fingerprint, Peptide,Fingerprint, Protein,Fingerprinting, Peptide,Fingerprinting, Protein,Mapping, Peptide,Peptide Fingerprint,Peptide Fingerprints,Protein Fingerprint,Protein Fingerprints
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D010768 Phosphoserine The phosphoric acid ester of serine. Serine Phosphate,Phosphorylserine,Seryl Phosphate,Phosphate, Serine,Phosphate, Seryl
D010769 Phosphothreonine The phosphoric acid ester of threonine. Used as an identifier in the analysis of peptides, proteins, and enzymes. Threonine Phosphate,Phosphate, Threonine
D010770 Phosphotransferases A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7. Kinases,Phosphotransferase,Phosphotransferases, ATP,Transphosphorylase,Transphosphorylases,Kinase,ATP Phosphotransferases
D011493 Protein Kinase C An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters. Calcium Phospholipid-Dependent Protein Kinase,Calcium-Activated Phospholipid-Dependent Kinase,PKC Serine-Threonine Kinase,Phospholipid-Sensitive Calcium-Dependent Protein Kinase,Protein Kinase M,Calcium Activated Phospholipid Dependent Kinase,Calcium Phospholipid Dependent Protein Kinase,PKC Serine Threonine Kinase,Phospholipid Sensitive Calcium Dependent Protein Kinase,Phospholipid-Dependent Kinase, Calcium-Activated,Serine-Threonine Kinase, PKC
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D004815 Epidermal Growth Factor A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form. EGF,Epidermal Growth Factor-Urogastrone,Urogastrone,Human Urinary Gastric Inhibitor,beta-Urogastrone,Growth Factor, Epidermal,Growth Factor-Urogastrone, Epidermal,beta Urogastrone

Related Publications

D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo.
September 1988, The Journal of biological chemistry,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
Epidermal growth factor receptor stimulation of diacylglycerol kinase.
March 1997, Biochemical and biophysical research communications,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
Diacylglycerol kinase delta regulates protein kinase C and epidermal growth factor receptor signaling.
October 2006, Proceedings of the National Academy of Sciences of the United States of America,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
The serine/threonine kinase cyclin G-associated kinase regulates epidermal growth factor receptor signaling.
July 2004, Proceedings of the National Academy of Sciences of the United States of America,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
In vivo and in vitro serine/threonine phosphorylations of epidermal growth factor receptor upon entry into the cell cycle.
January 1995, Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
Stimulation of epidermal growth factor receptor threonine 654 phosphorylation by platelet-derived growth factor in protein kinase C-deficient human fibroblasts.
May 1987, The Journal of biological chemistry,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
Identification of multiple epidermal growth factor-stimulated protein serine/threonine kinases from Swiss 3T3 cells.
July 1990, The Journal of biological chemistry,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
Role of threonine residues in regulation of the epidermal growth factor receptor by protein kinase C and mitogen-activated protein kinase.
July 1993, The Journal of biological chemistry,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
Isolation and characterization of two growth factor-stimulated protein kinases that phosphorylate the epidermal growth factor receptor at threonine 669.
August 1991, The Journal of biological chemistry,
D Schaap, and J van der Wal, and W J van Blitterswijk, and R L van der Bend, and H L Ploegh
C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.
February 1984, The Journal of biological chemistry,
Copied contents to your clipboard!