Abstract
According to the canonical scheme of reversible protein phosphorylation (fig. 1) protein kinases are normally silent, converter enzymes whose activation is triggered by a variety of impulses, mostly generated by extracellular signals. Due to such a role of “regulatable regulators” committed with the translation of signals into biochemical events, protein kinases can be classified after either their responsiveness to various stimuli or their capability to recognize definite structural features.
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Agostinis P, Goris J, Pinna LA, Marchiori F, Perich JW, Meyer HE and Merlevede W (1990) Synthetic peptides as model substrates for the study of the specificity of the polycation-stimulated protein phosphatase. Eur. J. Biochem. 189: 235–241
Ballou LM and Fischer EH (1986) Phosphoprotein phosphatases. In: The Enzymes Vol. XVII (Boyer PD and Krebs EG eds) Academic Press Inc. pp. 311–361
Beebe SJ and Corbin JD (1986) Cyclic nucleotide-dependent protein kinases. In: The Enzymes Vol. XVII ( Boyer PD and Krebs EG eds) Academic Press, Orlando pp. 44–111
Cooper JA (1990) The src family of protein tyrosine kinases. In: Peptides and protein phosphorylation ( Kemp BE ed) CRC Press Inc. Boca Raton pp. 85–113
Dayani N, McNaught RW, Shenolikar S and Smith RG (1990) Receptor interconversion model of hormone action, 2. Requirement of both kinase and phosphatase activities for conferring estrogen binding activity to the estrogen receptor. Biochem. 29: 2691–2698
Dent P, Lavoinne A, Nakielny S, Caudwell FB, Watt P and Cohen P (1990) The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle. Nature 348: 302–308
Dobrowolska G, Meggio F and Pinna LA (1987) Characterization of multiple forms of maize seedling protein kinases reminiscent of animal casein kinases S (type 1) and TS (type 2) Biochim. Biophys. Acta 931: 188–195
Donella-Deana A, Brunati AM, Marchiori F, Borin G and Pinna LA (1990) Different specificities of spleen tyrosine protein kinases as evidenced with synthetic peptide substrates Eur. J. Biochem. 194: 773–777
Draetta G (1990) Cell cycle control in eukariotes: molecular mechanism of cdc2 activation Trends Biochem. Sci. 15: 378–383
Fiol CJ, Mahrenholz AM, Roeske RW and Roach PJ (1987) Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase and glycogen synthase kinase 3. J. Biol. Chem. 262: 14042–14048
Flotow H, Graves PR, Wang A, Fiol CJ, Roeske RW and Roach PJ (1990) Phosphate groups as substrate determinants for casein kinase I action. J. Biol. Chem. 265: 14264–14269
Hardie DG, Carling D and Sim ATR (1989) The AMP-activated protein kinase: a multisubstrate regulator of lipid metabolism. Trends Biochem. Sci. 14: 20–23
Hunter T, Cooper JA (1985) Protein tirosine kinases. Ann. Rev. Biochem. 54: 897–930
Hunter T, Cooper JA (1986) Viral oncogenes and tyrosine phosphorylation. In: The Enzymes Vol. XVII ( Boyer PD and Krebs EG eds) Academic Press, Orlando pp. 192–246
Issinger OG, Martin T, Richter WW, Olson M and Fujiki H (1988) Hyperphosphorylation of N60, a protein structurally and immunologically related to nucleolin, after tumor-promoter treatment EMBO J. 7: 1621–1627
Masaracchia RA, Murdoch FE and Hassel TC (1990) Unique specificity determinants for an S6/H4 kinase and protein kinase-C.In: Peptides and Protein Phosphorylation ( Kemp BE ed) CRC Press Inc. Boca Raton pp. 189–207
Meggio F, Donella-Deana A and Pinna LA (1979) Studies on the structural requirements of a microsomal cAMP-independent protein kinase FEBS Lett. 106: 76–80
Meggio F, Perich JW, Meyer HE, Hoffmann-Posorske E, Lennon DPW, Johns RB and Pinna LA (1989) Synthetic fragments of -casein as model substrates for liver and mammary gland casein kinases. Eur. J. Biochem. 186: 459–464
Mercier JC (1981) Phosphorylation of caseins, present evidence for an aminoacid triplet code posttranslationally recognized by specific kinases. Biochimie 63: 1–17
Moore A, Boulton AP, Heid HW, Jarasch ED and Craig RK (1985) Purification and tissue specific expression of a casein kinase from the lactating guinea-pig mammary gland. Eur. J. Biochem. 152: 729–737
Nishizuka Y (1988) The molecular heterogeneity of protein kinase-C and its implications for cellular regulation. Nature 334: 661–665
Picton C, Woodgett J, Hemmings B and Cohen P (1984) Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Phosphorylation of site 5 by glycogen synthase kinase-5 (casein kinase II) is a prerequisite for phosphorylation of site 3 by glycogen synthase kinase-3. FEBS Lett. 150: 191–196
Pinna LA (1990) Casein kinase-2: An eminence grise in cellular regulation? Biochim. Biophys. Acta 1054: 267–284
Pinna LA, Agostinis P and Ferrari S (1986) Selectivity of protein kinases and protein phosphatases: a comparative analysis. Adv. Prot. Phosphatases 3: 327–368
Ralph RK, Darkin-Rattray S and Schofield P (1990) Growth-Related Protein kinases Bio Essays 12: 121–124
Reed LJ and Yeaman SJ (1987) Pyruvate dehydrogenase. In: The Enzymes Vol. XVIII ( Boyer PD and Krebs EG eds) Academic Press, Orlando pp. 77–95
Stull JT, Nunnally MH and Michnoff CH (1986) Calmodulin dependent protein kinases. In: The Enzymes Vol. XVII ( Boyer PD and Krebs EG eds) Academic Press, Orlando pp. 114–166
Ullrich A and Schlessinger J (1990) Signal transduction by receptors with tyrosine kinase activity. Cell 61: 203–212
Vulliet PR, Hall FL, Mitchell JP and Hardie DG (1989) Identification of a novel proline-directed serine/threonine protein kinase in rat pheochromocytoma. J. Biol. Chem. 264: 16292–16298
West DW (1986) Structure and function of the phosphorylated residues of casein. J. Dairy Res. 53: 333–352
Woodgett JR (1990) Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J. 9: 2431–2438
Zhang G, Stevens R and Leader DP (1990) The protein kinase encoded in the short unique region of pseudorobies virus: description of the gene and identification of its product in virions and in infected cells. J. Gen. Virol. 71: 1757–1765
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© 1991 Springer-Verlag Berlin Heidelberg
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Pinna, L.A. (1991). “Independent” Protein Kinases: A Challenge to Canons. In: Heilmeyer, L.M.G. (eds) Cellular Regulation by Protein Phosphorylation. NATO ASI Series, vol 56. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75142-4_22
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DOI: https://doi.org/10.1007/978-3-642-75142-4_22
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