Acknowledgement
Supported by : Korea Research Foundation, Korea Science and Engineering Foundation
References
- Colley, W.C., Sung, R., Jenco, R.L., Hammond, S.M., Altshuller, Y., Bar-Sagi, D., Morris, A.J., and Frohman, M.A. (1997). Phospholipase D2, a distinct phospholipase D isoform with novel regulatory properties that provokes cytoskeletal reorganization. Curr. Biol. 7, 191-201 https://doi.org/10.1016/S0960-9822(97)70090-3
- Desagher, S., Osen-Sand, A., Montessuit, S., Magnenat, E., Vilbois, F., Hochmann, A., Journot, L., Antonsson, B., and Martinou, J.C.(2001). Phosphorylation of Bid by casein kinases I and II regulates its cleavage by caspase 8. Mol. Cell 8, 601-611 https://doi.org/10.1016/S1097-2765(01)00335-5
- Exton, J.H. (1997). Phospholipase D: enzymology, mechanisms of regulation, and function. Physiol. Rev. 77, 303-320 https://doi.org/10.1152/physrev.1997.77.2.303
- Exton, J.H. (1999). Regulation of phospholipase D. Biochim. Biophys. Acta 1439, 121-133 https://doi.org/10.1016/S1388-1981(99)00089-X
- Freyberg, Z., Bourgoin, S., and Shields, D. (2002) Phospholipase D2 is localized to the rims of the Golgi apparatus in mammalian cells. Mol. Biol. Cell 13, 3930-3942 https://doi.org/10.1091/mbc.02-04-0059
- Ganley, I.G., Walker, S.J., Manifava, M., Li, D., Brown, H.A., and Ktistakis, N.T. (2001). Interaction of phospholipase D1 with a casein-kinase-2-like serine kinase. Biochem. J. 354, 369-378 https://doi.org/10.1042/0264-6021:3540369
- Gietz, R.D., Graham, K.C., and Litchfield, D.W. (1995). Interactions between the subunits of casein kinase II. J. Biol. Chem. 270, 13017-13021 https://doi.org/10.1074/jbc.270.22.13017
- Hammond, S.M., Altshuller, Y.M., Sung, T.C., Rudge, S.A., Ross, K., Engebrecht, J., Morris, A.J., and Frohman, M.A. (1995). Human ADP-ribosylation factor-activated phosphatidylcholinespecific phospholipase D defines a new and highly conserved gene family. J. Biol. Chem. 270, 29640-29643 https://doi.org/10.1074/jbc.270.50.29640
-
Hammond, S.M., Jenco, J.M., Nakashima, S., Cadwallader, K., Gu, Q.M., Cook, S., Nozawa, Y., Prestwich, G.D., Frohman, M.A., and Morris, A.J. (1997). Characterization of two alternately spliced forms of phospholipase D1: activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-
$\alpha$ . J. Biol. Chem. 272, 3860-3868 https://doi.org/10.1074/jbc.272.6.3860 - Hanna, D.E., Rethinaswamy, A., and Glover, C.V. (1995). Casein kinase II is required for cell cycle progression during G1 and G2/M in Saccharomyces cerevisiae. J. Biol. Chem. 270, 25905-25914 https://doi.org/10.1074/jbc.270.43.25905
- Hathaway, G.M., and Traugh, J.A. (1979). Cyclic nucleotideindependent protein kinases from rabbit reticulocytes. Purification of casein kinases. J. Biol. Chem. 254, 762-768
- Hui, L., Abbas, T., Pielak, R.M., Joseph, T., Bargonetti, J., and Foster, D.A. (2004). Phospholipase D elevates the level of MDM2 and suppresses DNA damage-induced increases in p53. Mol. Cell. Biol. 24, 5677-5686 https://doi.org/10.1128/MCB.24.13.5677-5686.2004
- Issinger, O.G. (1993). Casein kinases: pleiotropic mediators of cellular regulation. Pharmacol. Ther. 59, 1-30 https://doi.org/10.1016/0163-7258(93)90039-G
- Jakobi, R., and Traugh, J.A. (1992). Characterization of the phosphotransferase phosphotransferase domain of casein kinase II by site-directed mutagenesis and expression in Escherichia coli. J. Biol. Chem. 267, 23894-23902
- Kim, S.Y., Ahn, B.H., Min, K.J., Lee, Y.H., Joe, E.H., and Min, D.S. (2004). Phospholipase D isozymes mediate epigallocatechin gallate-induced cyclooxygenase-2 expression in astrocyte cells. J. Biol. Chem. 279, 38125-38133 https://doi.org/10.1074/jbc.M402085200
-
Kim, T.H., Lee, J.Y., Kang, B.S., and Bae, Y.S. (2005). In vitro characterization of protein kinase CKII
$\beta$ mutants defective in$\beta$ -$\beta$ dimerization. Mol. Cells 19, 124-130 - Krippner-Heidenreich, A., Talanian, R.V., Sekul, R., Kraft, R., Thole, H., Ottleben, H., and Luscher, B. (2001). Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1. Biochem. J. 358, 705-715 https://doi.org/10.1042/0264-6021:3580705
- Lin, W.J., Tuazon, P.T., and Traugh, J.A. (1991). Characterization of the catalytic subunit of casein kinase II expressed in Escherichia coli and regulation of activity. J. Biol. Chem. 266, 5664-5669
- Liscovitch, M., Czarny, M., Fiucci, G., and Tang, X. (2000). Phospholipase D: molecular and cell biology of a novel gene family. Biochem. J. 345, 401-415 https://doi.org/10.1042/0264-6021:3450401
- Litchfield, D.W. (2003). Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem. J. 369, 1-15 https://doi.org/10.1042/BJ20021469
- Min, D.S., Ahn, B.H., Rhie, D.J., Yoon, S.H., Hahn, S.J., Kim, M.S., and Jo, Y.H. (2001). Expression and regulation of phospholipase D during neuronal differentiation of PC12 cells. Neuropharmacology 41, 384-391 https://doi.org/10.1016/S0028-3908(01)00070-3
- Moon, I.S., Cho, S.J., Jin, I., and Walikonis, R. (2007). A simple method for combined fluorescence in situ hybridization and immunocytochemistry. Mol. Cells 24, 76-82
- Niefind, K., Guerra, B., Pinna, L.A., Issinger, O.G., and Schomburg, D. (1998). Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution. EMBO J. 17, 2451-2462 https://doi.org/10.1093/emboj/17.9.2451
- Pinna, L.A. (1990). Casein kinase 2: an 'eminence grise' in cellular regulation? Biochim. Biophys. Acta 1054, 267-284 https://doi.org/10.1016/0167-4889(90)90098-X
-
Seldin, D.C., and Leder, P. (1995). Casein kinase II
$\alpha$ transgeneinduced murine lymphoma: relation to theileriosis in cattle. Science 267, 894-897 https://doi.org/10.1126/science.7846532 - Shen, Y., Xu, L., and Foster, D.A. (2001). Role for phospholipase D in receptor-mediated endocytosis. Mol. Cell. Biol. 21, 595-602 https://doi.org/10.1128/MCB.21.2.595-602.2001
- Shin, S., Lee, Y., Kim, W., Ko, H., Choi, H., and Kim, K. (2005). Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8. EMBO J. 24, 3532-3542 https://doi.org/10.1038/sj.emboj.7600827
-
Zhang, C., Vilk, G., Canton, D.A., and Litchfield, D.W. (2002). Phosphorylation regulates the stability of the regulatory CK2
$\beta$ subunit. Oncogene 21, 3754-3764 https://doi.org/10.1038/sj.onc.1205467
Cited by
- The C-terminal domain of PLD2 participates in degradation of protein kinase CKII β subunit in human colorectal carcinoma cells vol.44, pp.9, 2009, https://doi.org/10.5483/bmbrep.2011.44.9.572