Overexpression of MARCKS, but not protein kinase C-α, increases phorbol ester-stimulated synthesis of phosphatidylcholine in human SK-N-MC neuroblastoma cells

Journal of Neurochemistry

Volumn 66, Issue 4, 1996, Pages 1766-1769

  Rose S D ^a   Morash, S C ^a   Ridgway, N D ^a   Byers, D M ^a   Cook, H W ^a  

^a DALHOUSIE UNIVERSITY   (Canada)

Author keywords

Myristoylated alanine rich protein kinase C substrate; Neuroblastoma cells; Phosphatidylcholine; Protein kinase C isoform

Indexed keywords

MARCKS PROTEIN; PHORBOL ESTER; PHOSPHATIDYLCHOLINE; PROTEIN KINASE C;

ARTICLE; ENZYME ACTIVATION; ENZYME SYNTHESIS; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; MOLECULAR CLONING; NEUROBLASTOMA CELL; PHOSPHOLIPID SYNTHESIS; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS REGULATION;

EID: 0029875281     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66041766.x     Document Type: Article

References (25)

1. Aderem A. (1992) The MARCKS brothers: a family of protein kinase C substrates. Cell 71, 713-716.
2. Allen L.-H. and Aderem A. (1995) Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in fibroblasts. EMBO J. 14, 1109-1121.
3. Balboa M. A., Balsinde J., Dennis E. A., and Insel P. A. (1995) A phospholipase D-mediated pathway for generating diacylglycerol in nuclei from Madin-Darby canine kidney cells. J. Biol. Chem. 270, 11738-11740.
4. Blackshear P. J. (1993) The MARCKS family of cellular protein kinase C substrates. J. Biol. Chem. 268, 1501-1504.
5. Byers D. M., Palmer F. B. St. C., Spence M. W., and Cook H. W. (1993) Dissociation of phosphorylation and translocation of a myristoylated protein kinase C substrate (MARCKS protein) in C6 glioma and N1E-115 neuroblastoma cells. J. Neurochem. 60, 1414-1421.
6. Conricode K. M., Smith J. L., Burns D. J., and Exton J. H. (1994) Phospholipase D activation in fibroblast membranes by the α and β isoforms of protein kinase C. FEBS Lett. 342, 149-153.
7. Cook H. W. and Vance D. E. (1985) Evaluation of possible mechanisms of phorbol ester stimulation of phosphatidylcholine synthesis in HeLa cells. Can J Biochem. Cell Biol. 63, 145-151.
8. Cook H. W., Byers D. M., Palmer F. B. St. C., and Spence M. W. (1989) Alterations of phospholipid metabolism by phorbol esters and fatty acids occur by different intracellular mechanisms in cultured glioma, neuroblastoma and hybrid cells. J. Biol. Chem 264, 2746-2752.
9. Erusalimsky J. D., Brooks S. F., Herget T., Morris C., and Rozengurt E. (1991) Molecular cloning and characterization of the acidic 80-kDa protein kinase C substrate from rat brain. Identification as a glycoprotein. J. Biol. Chem. 266, 7073-7080.
10. George T. P., Morash S. C., Cook H. W., Byers D. M., Palmer F. B. St. C., and Spence M. W. (1989) Phosphatidytcholine biosynthesis in cultured glioma cells: evidence for channeling of intermediates. Biochim. Biophys. Acta 1004, 283-291.
11. Hartwig J. H., Thelen M., Rosen A., Janmey P. A., Nairn A. C., and Aderem A. (1992) MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature 356, 618-622.
12. Herget T., Broad S., and Rozengurt E. (1994) Overexpression of the myristoylated alanine-rich C-kinase substrate in Rat1 cells increases sensitivity to calmodulin antagonists. Eur. J. Biochem. 225, 549-556.
13. Kent C. (1995) Eukaryotic phospholipid biosynthesis. Annu. Rev. Biochem. 64, 315-343.
14. Kim J., Shishido T., Jiang X., Aderem A., and McLaughlin S. (1994) Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles. J. Biol. Chem. 269, 28214-28219.
15. Liscovitch M., Ben-Av P., Danin M., Faiman G., Eldar H., and Livneh E. (1993) Phospholipase D-mediated hydrolysis of phosphatidylcholine: role in cell signalling. J. Lipid Mediat. 8, 177-182.
16. Nishizuka Y. (1992) Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258, 607-614.
17. Rosé S. D., Cook H. W., Palmer F. B. St. C., Ridgway N. D., and Byers D. M. (1994) Differential expression of MARCKS and other calmodulin-binding protein kinase C substrates in cultured neuroblastoma and glioma cells. J. Neurochem. 63, 2314-2323.
18. Sawai T., Negishi M., Nishigaki N., Ohno T., and Ichikawa A. (1993) Enhancement by protein kinase C of prostacyclin receptor-mediated activation of adenylate cyclase through a calmodulin/myristoylated alanine-rich C kinase substrate (MARCKS) system in IC2 mast cells. J. Biol. Chem. 268, 1995-2000.
19. Sheu F.-S., Huang F. L., and Huang K.-P. (1995) Differential responses of protein kinase C substrates (MARCKS, neuromodulin, and neurogranin) phosphorylation to calmodulin and S100. Arch. Biochem. Biophys. 316, 335-342.
20. Slack B. E., Breu J., Livneh E., Eldar H., and Wurtman R. J. (1995) Phorbol ester stimulates choline uptake in Swiss 3T3 fibroblasts following introduction of the gene encoding protein kinase Cα. Biochem. J. 305, 621-626.
21. Sproull S. A., Morash S. C., Byers D. M., Palmer F. B. St. C., and Cook H. W. (1995) Phorbol ester stimulation of phosphatidylcholine synthesis in four cultured neural cell lines: correlations with expression of protein kinase C isoforms. Neurochem Res. 20, 1397-1407.
22. Stumpo D. J., Bock C. B., Tuttle J. S., and Blackshear P. J. (1995) MARCKS deficiency in mice leads to abnormal brain development and perinatal death. Proc. Natl. Acad. Sci. USA 92, 944-948.
23. Swierczynski S. L. and Blackshear P. J. (1995) Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions. J Biol. Chem. 270, 13436-13445.
24. Toullec D., Pianetti P., Coste H., Bellevergue P., Grand-Perret T., Ajakane M., Baudet V., Boissin P., Boursier E., Loriolle F., Duhamel L., Charon D., and Kirilovsky J. (1991) The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C. J. Biol. Chem. 266, 15771-15781.
25. Vance D. E. (1991) Phospholipid metabolism and cell signalling in eucaryotes, in Biochemistry of Lipids, Lipoproteins and Membranes (Vance D. E. and Vance J. E., eds), pp. 205-240. Elsevier, New York.