Burns J. M. Jr., Parsons M., Rosman D. E., Reed S. G. (1993) Molecular cloning and characterizationof a 42-kDa protein phosphatase of Leishmania chagasi. J. Biol. Chem. 268: 17155–17161 Cohen P. (1989) The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58: 453–508  Delorme V., Cayla X., Faure G., Garcia A., Tardieux I. (2003) Actin dynamics is controlled by a casein kinase II and phosphatase 2C interplay on Toxoplasma gondii Toxofilin. Mol. Biol. Cell 14: 1900–1912 Dragesco A., Dragesco J., Coste F., Gasc C., Romestand B., Raymond J., Bouix G. (1995) Philasterides dicentrarchi, n. sp. (Ciliophora, Scuticociliatida), a histophagous opportunistic parasite of Dicentrachus labrax (Linnaeus. 1758), a reared marine fish. Eur. J. Protistol. 31: 327–340 Gaits F., Shiozaki K., Russell P. (1997) Protein phosphatase 2C acts independently of stress-activated kinase cascade to regulate the stress response in fission yeast. J. Biol. Chem. 272: 17873–17879 Gilbert L. A., Ravindran S., Turetzky J. M., Boothroyd J. C., Bradley P. J. (2007) Toxoplasma gondii targets a protein phosphatase 2C to the nuclei of infected host cells. Eukaryot. Cell 6: 73–83 Grothe K., Hanke C., Momayezi M., Kissmehl R., Plattner H., Schultz J. E. (1998) Functional characterization and localization of protein phosphatase type 2C from Paramecium. J. Bio. Chem. 273: 19167–19172 Hanada M., Kobayashi T., Ohnishi M., Ikeda S., Wang H., Katsura K., Yanagawa Y., Hiraga A., Kanamaru R., Tamura S. (1998) Selective suppression of stress-activated protein kinase pathway by protein phosphatase 2C in mammalian cells. FEBS Lett. 437: 172–176 Hanada M., Ninomiya-Tsuji J., Komaki K., Ohnishi M., Katsura K., Kanamaru R., Matsumoto K., Tamura S. (2001) Regulation of the TAK1 signaling pathway by protein phosphatase 2C. J. Biol. Chem. 276: 5753–5759 Huang L., Wong T. Y., Lin R. C., Furthmayr H. (1999) Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin. Regulation by conformational change. J. Biol. Chem. 274: 12803–12810 Hunter T. (2000) Signaling – 2000 and beyond. Cell 100: 113–127  Iglesias R., Parama A., Alvarez M. F., Leiro J., Fernandez J., Sanmartin M. L. (2001) Philasterides dicentrarchi (Ciliophora, Scuticociliatida) as the causative agent of scuticociliatosis in farmed turbot Scophthalmus maximus in Galicia (NW Spain). Dis. Aquat. Org. 46: 47–55 Jan G., Delorme V., David V., Revenu C., Rebollo A., Cayla X., Tardieux I. (2007) The toxofilin-actin-PP2C complex of Toxo plasma: identification of interacting domains. Biochem. J. 401: 711–719 Jung S. J., Kitamura S. I., Song J. Y., Oh M. J. (2007) Miamiensis avidus (Ciliophora: Scuticociliatida) causes systemic infection of olive flounder Paralichthys olivaceus and is a senior synonym of Philasterides dicentrarchi. Dis. Aquat. Org. 73: 227–234 Kim S. M., Cho J. B., Kim S. K., Nam Y. K., Kim K. H. (2004) Occurrence of scuticociliatosis in olive flounder Paralichthys olivaceus by Philasterides dicentrarchi (Ciliophora: Scuticociliatida). Dis. Aquat. Org. 62: 233–238 Klumpp S., Hanke C., Donella-Deana A., Beyer A., Kellner R., Pinna L. A., Schultz J. E. (1994) A membrane-bound protein phosphatase type 2C from Paramecium tetraurelia. J. Biol. Chem. 269: 32774–32780 Kumar K. A., Garcia C. R., Chandran V. R., Rooijen N. V., Zhou Y., Winzeler E., Nussenzweig V. (2007) Exposure of Plasmodium sporozoites to the intracellular concentration of potassium enhances infectivity and reduces cell passage activity. Mol. Biochem. Parasitol. 156: 32–40 Lammers T., Lavi S. (2007) Role of type 2C protein phosphatases in growth regulation and in cellular stress signaling. Crit. Rev. Biochem. Mol. Biol. 42: 437–461 Maeda T., Wurgler-Murphy S. M., Saito H. (1994) A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369: 242–245 Mamoun C. B., Sullivan D. J. Jr., Banerjee R., Goldberg D. E. (1998) Identification and characterization of an unusual double serine:threonine protein phosphatase 2C in the malaria parasite Plasmodium falciparum. J. Biol. Chem. 273: 11241–11247 McGowan C. H., Cohen P. (1998) Protein phosphatase-2C from rabbit skeletal muscle and liver: an Mg2+-dependent enzyme. Methods Enzymol. 159: 416–426 Meskiene I., Baudouin E., Schweighofer A., Liwosz A., Jonak C., Rodriguez P. L., Jelinek H., Hirt H. (2003) Stress-induced protein phosphatase 2C is a negative regulator of a mitogen-activated protein kinase. J. Biol. Chem. 278: 18945–18952 Mumby M. C., Walter G. (1993) Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth. Physiol. Rev. 73: 673–699 Noguchi M., Sasaki J. Y., Kamachi H., Inoue H. (2003) Protein phosphatase 2C is involved in the cAMP-dependent ciliary control in Paramecium caudatum. Cell Motil. Cytoskeleton 54: 95–104 Robinson M. K., Zyl W. H., Phizicky E. M., Broach J. R. (1994) TPD1 of Saccharomyces cerevisiae encodes a protein phosphatase 2C-like activity implicated in tRNA splicing and cell separation. Mol. Cell. Biol. 14: 3634–3645 Sheen J. (1998) Mutational analysis of protein phosphatase 2C involved in abscisic acid signal transduction in higher plants. Proc. Natl. Acad. Sci. USA 95: 975–980 Shenolikar S., Ingebritsen T. S. (1984) Protein (serine and threonine) phosphate phosphatases. Methods Enzymol. 107: 102–129 Shiozaki K., Russell P. (1995) Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase kinase homolog in the osmoregulation of fission yeast. EMBO J. 14: 492–502 Shiozaki K., Akhavan-niaki H., McGowan C. H., Russel P. (1994) Protein phosphatase 2C, encoded by ptc1+, is important in the heat shock response of Schizosaccharomyces pombe. Mol. Cell. Biol. 14: 3742–3751 Song J. Y., Kitamura S. I., Oh M. J., Kang H. S., Lee J. H., Tanaka S. J., Jung S. J. (2009) Pathogenicity of Miamiensis avidus (syn. Philasterides dicentrarchi), Pseudocohnilembus persalinus, Pseudocohnilembus hargisi and Uronema marinum (Ciliophora, Scuticociliatida). Dis. Aquat. Org. 83: 133–143 Tahtiharju S., Palva T. (2001) Antisense inhibition of protein phosphatase 2C accelerates cold acclimation in Arabidopsis thaliana. Plant J. 26: 461–470 Tamura S., Hanada M., Ohnishi M., Katsura K., Matsumoto K., Kobayashi T. (2002) Regulation of stress-activated protein kinase signaling pathways by protein phosphatases. Eur. J. Biochem. 269: 1060–1066 Tong Y., Quirion R., Shen S. H. (1998) Cloning and characterization of a novel mammalian PP2C isozyme. J. Biol. Chem. 273: 35282–35290