Mutational analysis of the regulatory mechanism of PKN: The regulatory region of PKN contains an arachidonic acid-sensitive autoinhibitory domain

Journal of Biochemistry

Volumn 126, Issue 3, 1999, Pages 475-484

  Yoshinaga, Chiho ^a   Mukai, Hideyuki ^a   Toshimori, Masanao ^a   Miyamoto, Masaaki ^a   Ono, Yoshitaka ^a  

^a KOBE UNIVERSITY   (Japan)

Author keywords

Arachidonic acid; I alpha; PKN; PRK2; Rho

Indexed keywords

ARACHIDONIC ACID; CYCLIC AMP DEPENDENT PROTEIN KINASE; MUTANT PROTEIN; PROTEIN KINASE; PROTEIN KINASE C;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; AUTOREGULATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME REGULATION; INSECT; NONHUMAN; STRUCTURE ACTIVITY RELATION;

ANIMALIA; INSECTA;

EID: 0032826336     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022476     Document Type: Article

References (49)

1. Mukai, H. and Ono, Y. (1994) A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C. Biochem. Biophys. Res. Commun. 199, 897-904
2. Kitagawa, M., Mukai, H., Shibata, H., and Ono, Y. (1995) Purification and characterization of a fatty acid-activated protein kinase (PKN) from rat testis. Biochem. J. 310, 657-664
3. Mukai, H., Kitagawa, M., Shibata, H., Takanaga, H., Mori, K., Shimakawa, M., Miyahara, M., Hirao, K., and Ono, Y. (1994) Activation of PKN, a novel 120-kDa protein kinase with leucine zipper-like sequences, by unsaturated fatty acids and by limited proteolysis. Biochem. Biophys. Res. Commun. 204, 348-356
4. Amano, M., Mukai, H., Ono, Y., Chihara, K., Matsui, T., Hamajima, Y., Okawa, K., Iwamatsu, A., and Kaibuchi, K. (1996) Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science 271, 648-650
5. Shibata, H., Mukai, H., Inagaki, Y., Homma, Y., Kimura, K., Kaibuchi, K., Narumiya, S., and Ono, Y. (1996) Characterization of the interaction between RhoA and the amino-terminal region of PKN. FEBS Lett. 385, 221-224
6. Watanabe, G., Saito, Y., Madaule, P., Ishizaki, T., Fujisawa, K., Morii, N., Mukai, H., Ono, Y., Kakizuka, A., and Narumiya, S. (1996) Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho. Science 271, 645-648
7. Peng, B., Morrice, N.A., Groenen, L.C., and Wettenhall, R.E. (1996) Phosphorylation events associated with different states of activation of a hepatic cardiolipin/protease-activated protein kinase. Structural identity to the protein kinase N-type protein kinases. J. Biol. Chem. 271, 32233-32240
8. Takahashi, M., Mukai, H., Toshimori, M., Miyamoto, M., and Ono, Y. (1998) Proteolytic activation of PKN by caspase-3 or related protease during apoptosis. Proc. Natl. Acad. Sci. USA 95, 11566-11571
9. Kitagawa, M., Shibata, H., Toshimori, M., Mukai, H., and Ono, Y. (1996) The role of the unique motifs in the amino-terminal region of PKN on its enzymatic activity. Biochem. Biophys. Res. Commun. 220, 963-968
10. 2+/calmodulin-independent activity of calmodulin-dependent protein kinase II by autophosphorylation. Autothiophosphorylation of the enzyme. J. Biol. Chem. 266, 11582-11588
11. Katoh, T. and Fujisawa, H. (1991) Autoactivation of calmodulin-dependent protein kinase II by autophosphorylation. J. Biol. Chem. 266, 3039-3044
12. Meyer, T., Hanson, P.I., Stryer, L., and Schulman, H. (1992) Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science 256, 1199-1202
13. 2+-independent activity. Proc. Natl. Acad. Sci. USA 85, 6337-6341
14. Hanks, S.K., Quinn, A.M., and Hunter, T. (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241, 42-52
15. Hanks, S.K. and Quinn, A.M. (1991) Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200, 38-62
16. Hunter, T. (1987) A thousand and one protein kinases. Cell 50, 823-829
17. 2+-calmodulin-dependent protein kinase Ia. J. Biol. Chem. 269, 2158-2164
18. 2+/calmodulin-dependent protein kinase IV kinase from rat brain. J. Biochem. 116, 923-930
19. 2+/calmodulin-dependent protein kinase kinase beta from rat cerebellum. J. Biochem. 121, 155-160
20. 2+-calmodulin-dependent protein kinase Ia kinase. Phosphorylation of threonine 196 is essential for activation. J. Biol. Chem. 270, 17616-17621
21. 2+/ calmodulin-dependent protein kinase IV. Identification of a brain CaM-kinase IV kinase. J. Biol. Chem. 269, 28640-28647
22. Alessi, D.R., James, S.R., Downes, C.P., Holmes, A.B., Gaffney, P.R., Reese, C.B., and Cohen, P. (1997) Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα. Curr. Biol. 7, 261-269
23. Stephens, L., Anderson, K., Stokoe, D., Erdjument, B.H., Painter, G.F., Holmes, A.B., Gaffney, P.R., Reese, C.B., McCormick, F., Tempst, P., Coadwell, J., and Hawkins, P.T. (1998) Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B. Science 279, 710-714
24. Mukai, H., Mori, K., Takanaga, H., Kitagawa, M., Shibata, H., Shimakawa, M., Miyahara, M., and Ono, Y. (1995) Xenopus PKN: cloning and sequencing of the cDNA and identification of conserved domains. Biochim. Biophys. Acta 1261, 296-300
25. Palmer, R.H., Ridden, J., and Parker, P.J. (1995) Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family. Eur. J. Biochem. 227, 344-351
26. Mukai, H., Toshimori, M., Shibata, H., Kitagawa, M., Shimakawa, M., Miyahara, M., Sunakawa, H., and Ono, Y. (1996) PKN associates and phosphorylates the head-rod domain of neurofilament protein. J. Biol. Chem. 271, 9816-9822
27. Ghayur, T., Hugunin, M., Talanian, R.V., Ratnofsky, S., Quinlan, C., Emoto, Y., Pandey, P., Datta, R., Huang, Y., Kharbanda, S., Allen, H., Kamen, R., Wong, W., and Kufe, D. (1996) Proteolytic activation of protein kinase C δ by an ICE/CED 3-like protease induces characteristics of apoptosis. J. Exp. Med. 184, 2399-2404
28. Ono, Y., Fujii, T., Ogita, 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
29. Kemp, B.E., Pearson, R.B., and House, C. (1983) Role of basic residues in the phosphorylation of synthetic peptides by myosin light chain kinase. Proc. Natl. Acad. Sci. USA 80, 7471-7475
30. Tallant, E.A., Wallace, R.W., and Cheung, W.Y. (1983) Purification and radioimmunoassay of calmodulin-dependent protein phosphatase from bovine brain. Methods Enzymol. 102, 244-256
31. Yazawa, M., Sakuma, M., and Yagi, K. (1980) Calmodulins from muscles of marine invertebrates, scallop and sea anemone. J. Biochem. 87, 1313-1320
32. Cazaubon, S.M. and Parker, P.J. (1993) Identification of the phosphorylated region responsible for the permissive activation of protein kinase C. J. Biol. Chem. 268, 17559-17563
33. Johnson, L.N., Noble, M.E., and Owen, D.J. (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158
34. Keranen, L.M., Dutil, E.M., and Newton, A.C. (1995) Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr. Biol. 5, 1394-1403
35. Taylor, S.S. and Radzio, A.E. (1994) Three protein kinase structures define a common motif. Structure 2, 345-355
36. Cazaubon, S., Bornancin, F., and Parker, P.J. (1994) Threonine-497 is a critical site for permissive activation of protein kinase C α. Biochem. J. 301, 443-448
37. Orr, J.W. and Newton, A.C. (1994) Requirement for negative charge on "activation loop" of protein kinase C. J. Biol. Chem. 269, 27715-27718
38. Mukai, H., Toshimori, M., Shibata, H., Takanaga, H., Kitagawa, M., Miyahara, M., Shimakawa, M., and Ono, Y. (1997) Interaction of PKN with α-actinin. J. Biol. Chem. 272, 4740-4746
39. Takanaga, H., Mukai, H., Shibata, H., Toshimori, M., and Ono, Y. (1998) PKN interacts with a paraneoplastic cerebellar degeneration-associated antigen, which is a potential transcription factor. Exp. Cell Res. 241, 363-372
40. Mellor, H., Flynn, P., Nobes, C.D., Hall, A., and Parker, P.J. (1998) PRK1 is targeted to endosomes by the small GTPase, RhoB. J. Biol. Chem. 273, 4811-4814
41. Palmer, R.H., Schonwasser, D.C., Rahman, D., Pappin, D.J., Herget, T., and Parker, P.J. (1996) PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. FEBS Lett. 378, 281-285
42. 2+-independent protein kinase Cs contain an amino-terminal domain similar to the C2 consensus sequence. Trends. Biochem. Sci. 18, 207-208
43. Dekker, L.V., McIntyre, P., and Parker, P.J. (1993) Mutagenesis of the regulatory domain of rat protein kinase C-η. A molecular basis for restricted histone kinase activity. J. Biol. Chem. 268, 19498-19504
44. Sossin, W.S., Fan, X., and Saberi, F. (1996) Expression and characterization of Aplysia protein kinase C: a negative regulatory role for the E region. J. Neurosci. 16, 10-18
45. Yedovitzky, M., Mochly, R.D., Johnson, J.A., Gray, M.O., Ron, D., Abramovitch, E., Cerasi, E., and Nesher, R. (1997) Translocation inhibitors define specificity of protein kinase C isoenzymes in pancreatic β-cells. J. Biol. Chem. 272, 1417-1420
46. Dekker, L.V. and Parker, P.J. (1997) Regulated binding of the protein kinase C substrate GAP-43 to the V0/C2 region of protein kinase C-δ. J. Biol. Chem. 272, 12747-12753
47. Quilliam, L.A., Lambert, Q.T., Mickelson, Y.L., Westwick, J.K., Sparks, A.B., Kay, B.K., Jenkins, N.A., Gilbert, D.J., Copeland, N.G., and Der, C.J. (1996) Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling. J. Biol. Chem. 271, 28772-28776
48. Vincent, S. and Settleman, J. (1997) The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization. Mol. Cell Biol. 17, 2247-2256
49. Stempka, L., Girod, A., Muller, H.J., Rincke, G., Marks, F., Gschwendt, M., and Bossemeyer, D. (1997) Phosphorylation of protein kinase Cδ (PKCδ) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCδ and an alanine 505 mutant in bacteria in a functional form. J. Biol. Chem. 272, 6805-6811