Regulation of protein kinase C

Current Opinion in Cell Biology

Volumn 9, Issue 2, 1997, Pages 161-167

  Newton, Alexandra C ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIACYLGLYCEROL; ISOENZYME; LIPID; PHORBOL ESTER; PHOSPHATIDYLSERINE; PROTEIN KINASE C;

ENZYME ACTIVATION; ENZYME BINDING; ENZYME CONFORMATION; ENZYME LOCALIZATION; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION;

EID: 0030987070     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80058-0     Document Type: Article

References (58)

1. Nishizuka Y: Protein kinase C and lipid signalling for sustained cellular responses. FASEB J 1995, 9:484-496. Comprehensive review of the signalling pathways that lead to protein kinase C activation.
2. Newton AC: Protein kinase C: structure, function, and regulation. J Biol Chem 1995, 270:28495-28498.
3. Dekker LV, Palmer RH, Parker PJ: The protein kinase C and protein kinase C related gene families. Curr Opin Struct Biol 1995, 5:396-402.
4. Newton AC: Protein kinase C: seeing two domains. Curr Biol 1995, 5:973-976.
5. Hurley JH, Newton AC, Parker PJ, Blumberg PM, Nishizuka Y: Taxonomy and function of C1 protein kinase C homology domains. Protein Sci 1997, in press. The authors align over 50 C1 domain sequences and define a consensus sequence that predicts whether particular C1 domains are typical (bind phorbol esters) or atypical (do not bind phorbol esters).
6. Zhang G, Kazanietz MG, Blumberg PM, Hurley JH: Crystal structure of the Cys2 activator-binding domain of protein kinase C δ in complex with phorbol ester. Cell 1995, 81:917-924. The authors elucidate the structure of the phorbol ester binding domain of protein kinase C 5 and establish that ligand binding regulates protein kinase C by altering the surface hydrophobicity of this domain rather than by inducing a conformational change.
7. Kazanietz MG, Wang S, Milne GWA, Lewin NE, Liu HL, Blumberg PM: Residues in the second cysteine-rich region of protein kinase C δ relevant to phorbol ester binding as revealed by site-directed mutagenesis. J Biol Chem 1995, 270:21852-21859.
8. Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL: The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site. Proc Natl Acad Sci USA 1996, 93:8312-8317. The authors elucidate the structure of an atypical C1 domain and show that one face of the phorbol-binding cavity is missing.
9. 2+-binding site.
10. 2+-binding site.
11. Essen L-O, Perisic O, Cheung R, Katan M, Williams RL: Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 1996, 380:595-602.
12. 2+-binding motif in C2 domains of synaptotagmin and protein kinase C. Science 1996, 273:248-251.
13. 2+ binding.
14. Hanks SK, Hunter T: The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 1995, 9:576-596. Comprehensive review of the protein kinase superfamily, with alignment of the primary sequence of 55 kinase cores.
15. Orr JW, Newton AC: Intrapeptide regulation of protein kinase C. J Biol Chem 1994, 269:8383-8387.
16. Srinivasan N, Bax B, Blundell TL, Parker PJ: Structural aspects of the functional modules in human protein kinase C α deduced from comparative analysis. Proteins 1996, 26:217-235.
17. Nishikawa K, Toker A, Johannes F-J, Songyang Z, Cantley LC: Determination of the specific substrate sequence motifs of protein kinase C isozymes. J Biol Chem 1997, 272:952-960. Identifies preferred substrate sequence motifs for nine protein kinase C isozymes and relates these to the predicted structure of the substrate-binding cavity.
18. Palmer RH, Dekker LV, Woscholski R, Le Good JA, Gigg R, Parker PJ: Activation of PRK1 by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-triphosphate. J Biol Chem 1995, 270:22412-22416.
19. Amano M, Mukai H, Ono Y, Chihara K, Matsui T, Hamajima Y, Okawa K, Iwamatsu A, Kaibuchi K: Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science 1996, 271:648-650.
20. Watanabe G, Saito Y, Madaule P, Ishizaki T, Fujisawa K, Morii N, Mukai H, Ono Y, Kakizuka A, Narumiya S: Protein kinase N (PKN) and PKN-related protein rhophilin as targets of small GTPase Rho. Science 1996, 271:645-647.
21. Newton AC: Cofactor regulation of protein kinase C. In Protein Kinase C. Edited by Dekker LV, Parker PJ. Austin, Texas: RG Landes; 1997:25-44.
22. Igarashi K, Kaneda M, Yamaji A, Saido T, Kikkawa U, Ono Y, Inoue K, Umeda M: A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody. J Biol Chem 1995, 270:29075-29078.
23. Khan WA, Blobe GC, Hannun YA: Arachidonic acid and free fatty acids as second messengers and the role of protein kinase C. Cell Signal 1995, 7:171-184.
24. Sando JJ, Chertihin OI: Activation of protein kinase C by lysophosphatidic acid: dependence on composition of phospholipid vesicles, Biochem J 1996, 317:583-588.
25. 2+.
26. Sharma R, Lee J, Wang S, Milne GWA, Lewin NE, Blumberg PM, Marquez VE: Conformationally constrained analogues of diacylglycerol. 10. Ultrapotent protein kinase C ligands based on a racemic 5-disubstituted tetrahydro-2-furanone template. J Med Chem 1996, 39:19-28.
27. Gilbert BA, Lim Y-H, Ding J, Badwey JA, Rando RR: Farnesyl thiotriazole, a potent neutrophil agonist and structurally novel activator of protein kinase C. Biochemistry 1995, 34:3916-3920.
28. Kazanietz MG, Barchi JJ, Omichinski JG, Blumberg PM: Low affinity binding of phorbol esters to protein kinase C and its recombinant cysteine-rich region in the absence of phospholipids. J Biol Chem 1995, 270:14679-14684. Shows that the binding of phorbol to the C1 domain does not require membrane lipids.
29. Luo J-H, Xing W-Q, Weinstein BI: The phorbol ester TPA markedly enhances the binding of calcium to the regulatory domain of protein kinase C βI in the presence of phosphatidylserine. Carcinogenesis 1995, 16:897-905.
30. Szallasi Z, Bogi K, Gohari S, Biro T, Acs P, Blumberg PM: Non-equivalent roles for the first and second zinc fingers of protein kinase C 5. Effect of their mutation on phorbol ester-induced translocation in NIH 3T3 cells. J Biol Chem 1996, 271:18299-18301. Demonstrates that the second C1 domain is the one that binds phorbol esters in vivo.
31. Tsutakawa SE, Medzihradszky KF, Flint AJ, Burlingame AL, Koshland DE Jr: Determination of in vivo phosphorylation sites in protein kinase C. J Biol Chem 1995, 270:26807-26812. Identifies the three in vivo phosphorylation sites of protein kinase C βII.
32. Keranen LM, Dutil EM, Newton AC: Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr Biol 1995, 5:1394-1403. Identifies the sites and function of the three in vivo phosphorylation sites of protein kinase Cs βII and α.
33. Cazaubon S, Bornancin F, Parker PJ: Threonine-497 is a critical site for permissive activation of protein kinase C α. Biochem J 1994, 301:443-448.
34. Orr JW, Newton AC: Requirement for negative charge on 'activation loop' of protein kinase C. J Biol Chem 1994, 269:27715-27718.
35. 1 and is essential for its activation. J Biol Chem 1994, 269:19578-19584.
36. Bornancin F, Parker PJ: Phosphorylation of threonine 638 critically controls the dephosphorylation and inactivation of protein kinase C α. Curr Biol 1996, 6:1114-1123.
37. Lee JY, Hannun YA, Obeid LM: Ceramide inactivates cellular protein kinase C α. J Biol Chem 1996, 271:13169-13174. Provides evidence that protein kinase C activity can be controlled in vivo by dephosphorylation.
38. Li W, Yu J-C, Shiin D-Y, Pierce JH: Characterization of a protein kinase C-δ (PKC-δ) ATP binding mutant J Biol Chem 1995, 270:8311-8318.
39. Soltoff SP, Toker A: Carbachol, substance P, and phorbol ester promote the tyrosine phosphorylation of protein kinase C 5 in salivary gland epithelial cells. J Biol Chem 1995, 271:13490-12495.
40. Denning MF, Dlugosz AA, Threadgill DW, Magnuson T, Yuspa SH: Activation of the epidermal growth factor receptor signal transduction pathway stimulates phosphorylation of protein kinase C 5. J Biol Chem 1996, 271:5325-5331.
41. Jaken S: Protein kinase C isozymes and substrates. Curr Opin Cell Biol 1996, 8:168-173. Concise review of isozyme-specific localization and substrates.
42. Newton AC: Protein kinase C: ports of anchor in the cell. Curr Biol 1996, 6:806-809.
43. Mochly-Rosen D: Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science 1995, 268:247-251. Review of targeting proteins for kinases, including a comprehensive review of protein kinase C binding proteins.
44. Ron D, Luo J, Mochly-Rosen D: C2 region-derived peptides inhibit translocation and function of β protein kinase C in vivo. J Biol Chem 1995, 270:24180-24187
45. Johnson JA, Mo G, Mochly-Rosen D: A protein kinase C inhibitor as an isozyme-selective antagonist of cardiac function. J Biol Chem 1996, 271:24982-24966. Demonstration that peptides derived from an amino-terminal variable region (V1) of protein kinase C ε can inhibit the phorbol ester dependent membrane translocation of this, but not other, isozymes of protein kinase C in permeabilized cardiac myocytes.
46. Chapline C, Mousseau B, Ramsay K, Duddy S, Li Y, Kiley SC, Jaken S: Identification of a major protein kinase C-binding protein and substrate in rat embryo fibroblasts. J Biol Chem 1996, 271:6417-6422.
47. Klauck TM, Faux MC, Labudda K, Langeberg LK, Jaken S, Scott JD: Coordination of three signalling enzymes by AKAP 79, a mammalian scaffold protein. Science 1996, 271:1589-1592. Demonstrates that protein kinase C is tethered to a mammalian scaffold protein that also anchors two other signalling enzymes, namely, calcineurin and protein kinase A.
48. Acs P, Szallasi Z, Kazanietz MG, Blumberg PM: Differential activation of PKC isozymes by 14-3-3 ζ protein. Biochem Biophys Res Commun 1995, 216:103-109.
49. Lehel C, Oláh Z, Jakab G, Szállási Z, Petrovics G, Harta G, Blumberg PM, Anderson WB: Protein kinase C ε subcellular localization domains and proteolytic degradation sites. J Biol Chem 1995, 270:19651-19658.
50. Prekeris R, Mayhew MW, Cooper JB, Terrian DM: Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function. J Cell Biol 1996, 132:77-90. Identifies an actin-binding region in the variable sequence between the first and second C1 domains of protein kinase C ε.
51. Blobe GC, Stribling DS, Fabbro D, Stabel S, Hannun YA: Protein kinase C βII specifically binds to and is activated by F-actin. J Biol Chem 1996, 271:15823-15830. Identifies an actin-binding motif in the variable sequence of the carboxyl terminus of protein kinase C βII.
52. Yeo E-J, Exton JH: Stimulation of phospholipase D by epidermal growth factor requires protein kinase C activation in Swiss 3T3 cells. J Biol Chem 1995, 270:3980-3988.
53. Lopez I, Burns DJ, Lambeth JD: Regulation of phospholipase D by protein kinase C in human neutrophils. J Biol Chem 1995, 270:19465-19472.
54. Balboa MA, Insel PA: Nuclear phospholipase D in Madin-Darby canine kidney cells. J Biol Chem 1995, 270:29843-29847
55. Kiss Z: Regulation of phospholipase D by protein kinase C. Chem Phys Lipids 1996, 80:81-102.
56. Singer WD, Brown HA, Jiang X, Sternweiw PC: Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity. J Biol Chem 1996, 271:4504-4510. Demonstrates that protein kinase C activates phospholipase D by a direct protein-protein interaction that is independent of a phosphotransfer reaction.
57. Cuvillier O, Pirianov G, Kleuser B, Vanek PG, Coso OA, Gutkind JS, Spiegel S: Suppression of ceramide-mediated programmed cell death by sphingosine-1 -phosphate. Nature 1996, 381:800-803. Demonstrates that protein kinase C is involved in ceramide-mediated apoptosis.
58. Parissenti AM, Kim SA, Colantonio CM, Snijura AL, Schimmer BP: Regulatory domain of human protein kinase C α dominantly inhibits protein kinase C β-I-regulated growth and morphology in Saccharomyces cerevisiae. J Cell Phys 1996, 166:609-617