Protein kinase activity

This method has been successfully applied to the substituted indole 2.6B, an analogue of the teleocidin type of protein kinase activators[ll]. 

FIGURE 23.22 The metabolic effects of insulin. As described in Chapter 34, binding of insulin to membrane receptors stimulates the protein kinase activity of the receptor. Subsequent phosphorylation of target proteins modulates the effects indicated. 

Bouaboula, M., Perrachon, S., Milligan, L., Canatt, X., Rinaldi-Carmona, M., Portier, M., Barth, F., Calandra, B., Pecceu, F., Lupker, J., Maffrand, J.-P., Le Fur, G., and Casellas, P. (1997). A selective inverse agonist for central cannabinoid receptor inhibits mitogen-activated protein kinase activation stimulated by insulin or insulin-like growth factor. J. Biol. Ckem. 272 22330-22339. 

Phosphorylation is a common method of regulation. As described above, SH2 domains bind to phosphorylated tyrosine residues. Conversely, phosphorylation of serines and threonines proximal to SH3 and PDZ domains uncouples them from their target motifs. Therefore modulation of protein kinase activity in cells regulates interactions between adaptor proteins and their target proteins. 

Fluorid ions stimulate bone formation by a direct mitogenic effect on osteoblasts mediated via protein kinase activation and other pathways. Further to these cellular effects, fluorides alter hydroxyapatite crystals in the bone matrix. In low doses, fluorides induce lamellar bone, while at higher doses abnormal woven bone with inferior quality is formed. The effect of fluorides on normal and abnormal (e.g. osteoporotic) bone therefore depends on the dose administered. 

Fluoride stimulates bone formation by protein kinase activation mediated effects on osteoblasts. Fluorides have been used in the treatment of osteoporosis, but their anti-fracture effect is not undisputed. 

Besides cytoplasmic protein kinases, membrane receptors can exert protein kinase activity. These so-called receptor tyrosine kinases (RTK) contain a ligandbinding extracellular domain, a transmembrane motif, and an intracellular catalytic domain with specificity for tyrosine residues. Upon ligand binding and subsequent receptor oligomerization, the tyrosine residues of the intracellular domain become phosphory-lated by the intrinsic tyrosine kinase activity of the receptor [3, 4]. The phosphotyrosine residues ftmction as docking sites for other proteins that will transmit the signal received by the RTK. 

Jurivich, D. A., Chung, J., Blenis, J. (1991). Heat shock induces two distinct S6 protein kinase activities in quiescent mammalian fibroblasts. J. Cell. Physiol. 148,252-259. 

Protein kinase activities wete originally described as being cAMP-dependent or cAMP-independent. This... 

II. PROTEIN KINASE ACTIVITY AND REGULATION OF CELL CYCLE EVENTS IN THE YEAST AND SELECTED VERTEBRATE MODEL SYSTEMS... 

B. Regulators of Cdc2/Cdk2 Protein Kinase Activity Cyclins... 

Choi, T., Aoki, E, Mori, M., Yamashita, M., Nagahama, Y., and Kohmoto, K. (1991). Activation of p34nfc2 protein kinase activity in meiotic and mitotic cell cycles in mouse oocytes and embryos. Development 113 789-795. 

Morrison, D. K., Kaplan, D. R., Rapp, U., and Roberts, T. M. (1988). Signal transduction from membrane to cytoplasm growth factors and membrane-bound oncogene products increase Raf-1 phosphorylation and associated protein kinase activity. Proc. Natl. Acad. Sci. USA 85 8855-8859. 

Stokoe, D., Campbell, D. G., Nakielny, S., Hidaka, H., Leevers, S. J., Marshall, C., and Cohen, P. (1992). MAPKAPkinase-2 a novel protein kinase activated by mitogen-activated protein kinase. EMBO J. 11 3985-3994. 

Bode, A.M. and Dong, Z. 2003. Mitogen-activated protein kinase activation in UV-induced signal transduction. 

Nestler E. Under seige the brain and opiates. Neuron 1996 16 897—900. Nestler E, Tallman J. Chronic morphine treatment increases cAMP dependent protein kinase activity in the rat locus coeruleus. Mol Pharmacol 1988 33 127-132. 

Hitti, E., Iakovleva, T., Brook, M., Deppenmeier, S., Gruber, A. D., Radzioch, D., Clark, A. R., Blackshear, P. J., Kotlyarov, A., and Gaestel, M. (2006). Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element. Mol. Cell Biol. 26, 2399—2407. 

Lali, F. V., Hunt, A. E., Turner, S. J., and Foxwell, B. M. (2000). The pyridinyl imidazole inhibitor SB203580 blocks phosphoinositide-dependent protein kinase activity, protein kinase B phosphorylation, and retinoblastoma hyperphosphorylation in interleukin-2-stimulated T cells independendy ofp38 mitogen-activated protein kinase. J. Biol. Chem. 275, 7395-7402. 

Poteet-Smith, C. E., Smith, J. A., Lannigan, D. A., Freed, T. A., and Sturgill, T. W. (1999). Generation of constitutively active p90 ribosomal S6 kinase in vivo. Implications for the mitogen-activated protein kinase-activated protein kinase family. J. Biol. Chem. 274, 22135-22138. 

Sharma, V., Wang, Q. and Lawrence, D. S. (2008). Peptide-based fluorescent sensors of protein kinase activity Design and applications. Biochim Biophys. Acta. 1784, 94—99. 

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