Abstract
The existence of multiple isozymes of protein kinase C (PKC) raised a new question of whether each PKC isozyme has a specific function (1–7). The activation mechanism of each PKC isozyme is clearly different among the three subgroups, conventional PKC, novel PKC, and atypical PKC, but that of each isozyme in a subgroup has not been clarified (1–8). Many reports have demonstrated that a certain cellular response is regulated by a specific PKC isozyme, although the molecular mechanisms of PKC function in defined cellular responses has not been clarified.
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References
Nishizuka, Y. (1984) The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 308, 693–698.
Nishizuka, Y. (1986) Studies and perspectives of protein kinase C. Science 233, 305–312.
Nishizuka, Y. (1992) Intracellular signalling by hydrolysis of phospholipids and activation of protein kinase C. Science 258, 607–614.
Ono, Y., Kikkawa, U., Ogita, K., Fujii, T., Kurokawa, T., Asaoka, Y., et al. (1987) Expression and properties of two types of protein kinase C determined by alternative splicing from a single gene. Science 236, 1116–1120.
Ono, Y., Fujii, T., Ogia, K., Kikkawa, U., Igarashi, K., and Nishizuka, Y. (1988) The structure, expression, and properties of additional members of the protein kinase C family. J. Biol. Chem. 263, 6927–6932.
Ono, Y., Fujii, T., Ogita, K., Kikkawa, U., Igarashi, K., and Nishizuka, Y. (1989) Protein kinase C ζ subspecies from rat brain: its structure, expression and properties. Proc. Natl. Acad. Sci. USA 86, 3099–3103.
Osada, S., Mizuno, K., Saido, T. C, Akita, Y., Suzuki, K., Kuroki, T., et al. (1990) A phorbol ester receptor/protein kinase, nPKCη? a new member of the protein kinase C family predominantly expressed in lung and skin. J. Biol. Chem. 265, 22,434–22,440.
Nishizuka, Y (1995) Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9, 484–496.
Sakai, N., Sasaki, K., Ikegaki, N., Shirai, Y, and Saito, N. (1997) Direct visualization of translocation of γ-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein. J. Cell Biol. 139, 1465–1476.
Oancea, E., Teruel, M., Quest, A., and Meyer, T. (1998) Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J. Cell Biol. 140, 485–498.
Oancea, E. and Meyer, T. (1998) Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell 95, 307–318.
Shirai, Y, Kashiwagi, K., Yagi, K., Sakai, N., and Saito, N. (1998) Distinct effects of fatty acids on translocation of γ-and ε-protein kinase C. J. Cell. Biol. 143, 511–521.
Ohmori, S., Shirai, Y, Sakai, N., Fujii, M., Konishi, H., Kikkawa, U., et al. (1998) Three distinct mechanisms for translocation and activation of ζ-subspecies of protein kinase C. Mol. Cell. Biol. 18, 5263–5271.
Kajimoto, T., Ohmori, S., Shirai, Y, Sakai, N., and Saito, N. (2001) Subtype-specific translocation of the 6 subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells. Mol. Cell. Biol. 21, 1769–1783
Almholt, K., Arkhammar, P. O. G., Thastrup, O., Tullin, S. (1999) Simultaneous visualization of the translocation of protein kinase Cα-green fluorescent protein hybrids and intracellular calcium concentrations. Biochem. J. 337, 211–218
Feng, X., Zhang, J., Barak, L. S., Meyer, T., Caron, M. G., and Hannun, Y A. (1998) Visualization of dynamic trafficking of a protein kinase C βII/green fluorescent protein conjugate reveals differences in G protein-coupled receptor activation and desensitization J. Biol. Chem. 273, 10,755–10,762.
Wang, Q. J., Bhattacharyya, D., Garfield, S., Nacro, K., Marquez, V. E., and Blumberg, P. M. (1999) Differential localization of protein kinase CS by phorbol esters and related compounds using a fusion protein with green fluorescent protein. J. Biol. Chem. 274, 37,233–37,239.
Wang, Q. J., Fang, T-W, Fenick, D., Garfield, S., Bienfait, B., Marquez, V. E., et al. (2000) The Lipophilicity of phorbol esters as a critical factor in determining the pattern of translocation of protein kinase CS fused to green fluorescent protein. J. Biol. Chem. 275, 12,136–12,146.
Shirai, Y, Segawa, S., Kuriyama, M., Goto, K., Sakai, N., and Saito, N. (2000) Subtype-specific translocation of diacylglycerol kinase α and β and its correlation with protein kinase C. J. Biol. Chem. 275, 24,760–24,766.
Zeidman, R., Löfgren, B., Påhlman, S., and Larsson, C. (1999) PKCε, via its regulatory domain and independently of its catalytic domain, induces neurite-like processes in neuroblastoma cells. J. Cell Biol. 145, 713–726.
Kashiwagi, K., Shirai, Y., Kuriyama, M., Sakai, N., and Saito, N. (2002) Importance of C1B domain for lipid messenger-induced targeting of PKC. J. Biol. Chem. 277, 18,037–18,045.
Matz, M. V., Fradkov, A. F., Labas, Y. A., Savitsky, A. P., Zaraisky, A. G., Markelov, M. L., et al. (1999) Fluorescent proteins from nonbioluminescent Anthozoa species. Nat. Biotechnol. 17, 969–973.
Baird, G. S., Zacharias, D. A., and Tsien, R. Y. (2000) Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. USA 97, 11,984–11,989.
Newton, A. C. (1997) Regulation of protein kinase C. Curr. Opin Cell Biol. 9, 161–167.
Campbell, R. E., Tour, O., Palmer, A. E., Steinbach, P. A., Baird, G. S., Zacharias, D. A., et al. (2002) A monomeric red fluorescent protein. Proc. Natl. Acad. Sci. USA 99, 7877–7882.
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Saito, N. (2003). Fluorescence Imaging of Protein Kinase C Translocation in Living Cells. In: Newton, A.C. (eds) Protein Kinase C Protocols. Methods in Molecular Biology™, vol 233. Humana Press. https://doi.org/10.1385/1-59259-397-6:93
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DOI: https://doi.org/10.1385/1-59259-397-6:93
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Print ISBN: 978-1-58829-068-7
Online ISBN: 978-1-59259-397-2
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