Abstract
There is increasing evidence that protein kinase CK2 is involved, among a wide variety of cellular processes, in the maintenance of mammalian cell morphology and cell polarity. Here, we show that in epithelial cells, a fraction of CK2 is associated to the plasma membrane and that this localization is controlled by cell–matrix interactions. In addition, inhibition of CK2 activity in mammary epithelial cells (MCF10A), using either the specific CK2 inhibitor TBB or siRNA-mediated CK2β knockdown, induced differential phenotypes revealing an important role of this enzyme in epithelial cell morphology.
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References
Landesman-Bollag E, Channavajhala PL, Cardiff RD, Seldin DC (1998) p53 deficiency and misexpression of protein kinase CK2alpha collaborate in the development of thymic lymphomas in mice. Oncogene 16:2965–2974. doi:10.1038/sj.onc.1201854
Landesman-Bollag E, Romieu-Mourez R, Song DH, Sonenshein GE, Cardiff RD, Seldin DC (2001) Protein kinase CK2 in mammary gland tumorigenesis. Oncogene 20:3247–3257. doi:10.1038/sj.onc.1204411
Meggio F, Pinna LA (2003) One-thousand-and-one substrates of protein kinase CK2? FASEB J 17:349–368. doi:10.1096/fj.02-0473rev
Niefind K, Guerra B, Ermakowa I, Issinger OG (2001) Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. EMBO J 20:5320–5231. doi:10.1093/emboj/20.19.5320
Filhol O, Nueda A, Martel V, Gerber-Scokaert D, Benitez MJ, Souchier C et al (2003) Live-cell fluorescence imaging reveals the dynamics of protein kinase CK2 individual subunits. Mol Cell Biol 23:975–987. doi:10.1128/MCB.23.3.975-987.2003
Filhol O, Martiel JL, Cochet C (2004) Protein kinase CK2: a new view of an old molecular complex. EMBO Rep 5:351–355. doi:10.1038/sj.embor.7400115
Canton DA, Litchfield DW (2006) The shape of things to come: an emerging role for protein kinase CK2 in the regulation of cell morphology and the cytoskeleton. Cell Signal 18:267–275. doi:10.1016/j.cellsig.2005.07.008
Pagano MA, Andrzejewska M, Ruzzene M, Sarno S, Cesaro L, Bain J et al (2004) Optimization of protein kinase CK2 inhibitors derived from 4,5,6,7-tetrabromobenzimidazole. J Med Chem 47:6239–6247. doi:10.1021/jm049854a
Debnath J, Muthuswamy SK, Brugge JS (2003) Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in three-dimensional basement membrane cultures. Methods 30:256–268. doi:10.1016/S1046-2023(03)00032-X
Filhol-Cochet O, Loue-Mackenbach P, Cochet C, Chambaz EM (1994) Casein kinase 2 and the cell response to growth factors. Cell Mol Biol Res 40:529–537
Laramas M, Pasquier D, Filhol O, Ringeisen F, Descotes JL, Cochet C (2007) Nuclear localization of protein kinase CK2 catalytic subunit (CK2alpha) is associated with poor prognostic factors in human prostate cancer. Eur J Cancer 43:928–934. doi:10.1016/j.ejca.2006.11.021
Orford K, Crockett C, Jensen JP, Weissman AM, Byers SW (1997) Serine phosphorylation-regulated ubiquitination and degradation of beta-catenin. J Biol Chem 272:24735–24738. doi:10.1074/jbc.272.40.24735
Seger D, Gechtman Z, Shaltiel S (1998) Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading. J Biol Chem 273:24805–24813. doi:10.1074/jbc.273.38.24805
Yin X, Jedrzejewski PT, Jiang JX (2000) Casein kinase II phosphorylates lens connexin 45.6 and is involved in its degradation. J Biol Chem 275:6850–6856. doi:10.1074/jbc.275.10.6850
Raman C, Kuo A, Deshane J, Litchfield DW, Kimberly RP (1998) Regulation of casein kinase 2 by direct interaction with cell surface receptor CD5. J Biol Chem 273:19183–19189. doi:10.1074/jbc.273.30.19183
Lickert H, Bauer A, Kemler R, Stappert J (2000) Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell–cell adhesion. J Biol Chem 275:5090–5095. doi:10.1074/jbc.275.7.5090
Serres M, Filhol O, Lickert H, Grangeasse C, Chambaz EM, Stappert J et al (2000) The disruption of adherens junctions is associated with a decrease of E-cadherin phosphorylation by protein kinase CK2. Exp Cell Res 257:255–264. doi:10.1006/excr.2000.4895
Sarrouilhe D, Filhol O, Leroy D, Bonello G, Baudry M, Chambaz EM et al (1998) The tight association of protein kinase CK2 with plasma membranes is mediated by a specific domain of its regulatory beta-subunit. Biochim Biophys Acta 1403:199–210. doi:10.1016/S0167-4889(98)00038-X
Stigare J, Buddelmeijer N, Pigon A, Egyhazi E (1993) A majority of casein kinase II alpha subunit is tightly bound to intranuclear components but not to the beta subunit. Mol Cell Biochem 129:77–85. doi:10.1007/BF00926578
Faust M, Jung M, Gunther J, Zimmermann R, Montenarh M (2001) Localization of individual subunits of protein kinase CK2 to the endoplasmic reticulum and to the Golgi apparatus. Mol Cell Biochem 227:73–80. doi:10.1023/A:1013129410551
Duncan JS, Gyenis L, Lenehan J, Bretner M, Graves LM, Haystead TA, et al (2008) An unbiased evaluation of CK2 inhibitors by chemo-proteomics: characterization of inhibitor effects on CK2 and identification of novel inhibitor targets. Mol Cell Proteomics 7:1077–1088. doi:10.1074/mcp.M700559-MCP200
Acknowledgments
This work was supported by grants from the Institut National de la Santé et de la Recherche Médicale (INSERM), the Commissariat à l’Energie Atomique, Association pour la Recherche sur le Cancer (ARC) and the Ligue Nationale contre le Cancer (équipe labellisée 2007).
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Deshière, A., Theis-Febvre, N., Martel, V. et al. Protein kinase CK2 and cell polarity. Mol Cell Biochem 316, 107–113 (2008). https://doi.org/10.1007/s11010-008-9845-y
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DOI: https://doi.org/10.1007/s11010-008-9845-y