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Xu X, Landesman-Bollag E, Channavajhala PL, Seldin DC (1999) Murine protein kinase CK2: gene and oncogene.

Pinna LA (2003) The raison d’etre of constitutively active protein kinase: the lesson of CK2. Guerra B, Boldyreff B, Sarno S, Cesaro L, Issinger OG, Pinna LA (1999) CK2: a protein kinase in need of control. Olsten ME, Litchfield DW (2004) Order or chaos? An evaluation of the regulation of protein kinase CK2. doi: 10.1096/fj.02-0473revįilhol O, Martiel J-L, Cochet C (2004) Protein kinase CK2: a new view of an old molecular complex. Meggio F, Pinna LA (2003) One-thousand-and-one substrates of protein kinase CK2? FASEB J 17:349–368. Guerra B, Issinger OG (1999) Protein kinase CK2 and its role in cellular proliferation, development and pathology. Litchfield DW (2003) Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Pinna LA, Meggio F (1997) Protein kinase CK2 (“casein kinase-2”) and its implication in cell division and proliferation. These results show that the anti-Cdc37 antibody can be a promising new tool to evaluate in vivo CK2 activity. However, cellular apoptotic stresses, such as anisomycin treatment and UV irradiation, were found to rather modestly increase phosphorylation of Cdc37 on Ser13. CK2 inhibitors are known to induce cell apoptosis, suggesting a reverse correlation between cell apoptosis and CK2 activity. While CK2 is suggested to be involved in cell proliferation, mitogenic stimulation of starved cells by fresh serum or insulin-like growth factor-I did not enhance phosphorylation of Cdc37 on Ser13. Treatment of cells with TBB resulted in the decrease in the phosphorylation level of endogenous Cdc37 on Ser13, as revealed by anti-Cdc37, and overexpression of either CK2α or CK2β subunit enhanced the Cdc37 phosphorylation level. Immunoblotting with this antibody showed that heparin and 4,5,6,7-tetrabromobenzotriazole (TBB), known CK2 inhibitors, inhibited in vitro phosphorylation of Cdc37 on Ser13 by CK2 holoenzyme or CK2α, confirming the specificity of the antibody to detect CK2 activity. Here we investigated CK2 activity both in vitro and in cultured cells by using anti-Cdc37 antibody. We have recently produced an anti-Cdc37 antibody which specifically recognizes Cdc37 that is phosphorylated on Ser 13. CK2-dependent phosphorylation of a kinase-specific Hsp90 co-chaperone Cdc37 on a conserved serine residue (Ser13) is essential for the function of Cdc37.