Protein kinase C isozymes and substrates

Current Opinion in Cell Biology

Volumn 8, Issue 2, 1996, Pages 168-173

  Jaken, Susan ^a  

^a Adirondack Biomedical Research Institute Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ISOENZYME; PROTEIN KINASE C;

CELL FUNCTION; CELL TYPE; ENZYME SUBSTRATE; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN TARGETING; SHORT SURVEY;

EID: 0029965696     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80062-7     Document Type: Article

References (58)

1. Nishizuka Y: Protein kinases 5: protein kinase C and lipid signaling for sustained cellular responses. FASEB J 1995, 9:484-496. This is a comprehensive review of the production of lipid mediators and of PKC activation.
2. Van Lint J, Sinnett-Smith J, Rozengurt E: Expression and characterization of PKD, a phorbol ester and diacylglycerol-stimulated serine protein kinase. J Biol Chem 1995, 270:1455-1461.
3. Johannes F-J, Prestle J, Dieterich S, Oberhagemann P, Link G, Pfizenmaier K: Characterization of activators and inhibitors of protein kinase Cμ. Eur J Biochem 1995, 227:303-307.
4. Nakanishi H, Brewer KA, Exton JH: Activation of the ζ-isozyme of protein kinase-C by phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 1993, 268:13-16.
5. Toker A, Meyer M, Reddy KK, Falck JR, Aneja R, Aneja S, Parra A, Burns DJ, Ballas LM, Cantley LC: Activation of protein kinase C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5-P3. J Biol Chem 1995, 270:32358-32366.
6. 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-trisphosphate - a comparison with protein kinase C isotypes. J Biol Chem 1995, 270:22412-22416.
7. Ahmed S, Lee J, Kozma R, Best A, Monfries C, Lim L: A novel functional target for tumor-promoting phorbol esters and lysophosphatidic acid. J Biol Chem 1993, 268:10709-10712.
8. Kazanietz MG, Lewin NE, Bruns JD, Blumberg PM: Characterization of the cysteine-rich region of the Caenorhabditis elegans protein unc-13 as a high affinity phorbol ester receptor. J Biol Chem 1995, 270:10777-10783.
9. Clark KJ, Murray AW: Evidence that the bradykinin-induced activation of phospholipase D and of the mitogen-activated protein kinase cascade involve different protein kinase C isoforms. J Biol Chem 1995, 270:7097-7103.
10. Ha KS, Exton JH: Differential translocation of protein kinase C isozymes by thrombin and platelet-derived growth factor. A possible function for phosphatidylcholine-derived diacylglycerol. J Biol Chem 1993, 268:10534-10539.
11. Olivier AR, Parker PJ: Bombesin, platelet-derived growth factor, and diacylglycerol induce selective membrane association and down-regulation of protein kinase C isotypes in Swiss 3T3 cells. J Biol Chem 1994, 269:2758-2763.
12. Clerk A, Bogoyevitch MA, Andersson MB, Sugden PH: Differential activation of protein kinase C isoforms by endothelin-1 and phenylephrine and subsequent stimulation of p42 and p44 mitogen-activated protein kinases in ventricular myocytes cultured from neonatal rat hearts. J Biol Chem 1994, 269:32848-32857.
13. Goss VL, Hocevar BA, Thompson LJ, Stratton CA, Burns DJ, Fields AP: Identification of nuclear βII protein kinase C as a mitotic lamin kinase. J Biol Chem 1994, 269:19074-19080.
14. Jones MJ, Murray AW: Evidence that ceramide selectively inhibits protein kinase C-α translocation and modulates bradykinin activation of phospholipase D. J Biol Chem 1995, 270:5007-5013.
15. Müller G, Ayoub M, Storz P, Rennecke J, Fabbro D, Pfizenmaier K: PKC ζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid. EMBO J 1995, 14:1961-1969.
16. Kazanietz MG, Areces LB, Bahador A, Mischak H, Goodnight J, Mushinski JF, Blumberg PM: Characterization of ligand and substrate specificity for the calcium-dependent and calcium-independent protein kinase-C isozymes. Mol Pharmacol 1993, 44:298-307.
17. Kielbassa K, Müller H-J, Meyer HE, Marks F, Gschwendt M: Protein kinase Cδ-specific phosphorylation of the elongation factor eEF-1a and an eEF-1a peptide at threonine 431. J Biol Chem 1995, 270:6156-6162.
18. Municio MM, Lozano J, Sánchez P, Moscat J, Diaz-Meco MT: Identification of heterogeneous ribonucleoprotein A1 as a novel substrate for protein kinase C zeta. J Biol Chem 1995, 270:15884-15891.
19. Goodnight J, Mischak H, Kolch W, Mushinski JF: Immunocytochemical localization of eight protein kinase C isozymes overexpressed in NIH 3T3 fibroblasts. Isoform-specific association with microfilaments, Golgi, endoplasmic reticulum, and nuclear and cell membranes. J Biol Chem 1995, 270:9991-10001.
20. Lehel C, Olah Z, Jakab G, Anderson WB: Protein kinase C ε is localized to the Golgi via its zinc-finger domain and modulates Golgi function. Proc Natl Acad Sci USA 1995, 92:1406-1410.
21. Kiley SC, Parker PJ: Differential localization of protein kinase C isozymes in U937 cells: evidence for distinct isozyme functions during monocyte differentiation. J Cell Sci 1995, 108:1003-1016.
22. Liao L, Ramsay K, Jaken S: Protein kinase C isozymes in progressively transformed rat embryo fibroblasts. Cell Growth Differ 1994, 5:1185-1194.
23. Hyatt SL, Liao L, Chapline C, Jaken S: Identification and characterization of α-protein kinase C binding proteins in normal and transformed REF52 cells. Biochemistry 1994, 33:1223-1228.
24. Liao L, Hyatt SL, Chapline C, Jaken S: Protein kinase C domains involved in interactions with other proteins. Biochemistry 1994, 33:1229-1233.
25. Chapline C, Ramsay K, Klauck T, Jaken S: Interaction cloning of protein kinase C substrates. J Biol Chem 1993, 268:6858-6861.
26. Dong L, Chapline C, Mousseau B, Fowler L, Ramsay K, Stevens JL, Jaken S: 35H, a sequence isolated as a protein kinase C binding protein, is a novel member of the adducin family. J Biol Chem 1995, 270:25534-25540. Phosphorylation of PKC-binding proteins reduces their affinity for PKC; thus, phosphorylation provides a reversible mechanism for regulating PKC/binding protein associations. Phosphorylation also decreases PS binding to γ adducin and causes γ adducin to redistribute from cytoskeletal to soluble subcellular fractions.
27. Hyatt SL, Liao L, Aderem A, Naim A, Jaken S: Correlation between protein kinase C binding proteins and substrates in REF52 cells. Cell Growth Differ 1994, 5:495-502.
28. Mochly-Rosen D: Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science 1995, 268:247-251. This is a review of the identification and roles of targeting proteins in regulating PKC, PKA and calcium-calmodulin kinase pathways.
29. Ron D, Chen C, Caldwell J, Jamieson L, Orr E, Mochly-Rosen D: Cloning of an intracellular receptor for protein kinase C: a homolog of the β subunit of G proteins. Proc Natl Acad Sci USA 1994, 91:839-843.
30. Staudinger J, Zhou J, Burgess R, Elledge SJ, Olson EN: PICK1: a perinuclear binding protein and substrate for protein kinase C isolated by the yeast two-hybrid system. J Cell Biol 1995, 128:263-271.
31. Germano P, Gomez J, Kazanietz MG, Blumberg PM, Rivera J: Phosphorylation of the γ chain of the high affinity receptor for immunoglobulin E by receptor-associated protein kinase C-δ. J Biol Chem 1994, 269:23102-23107.
32. Haleem-Smith H, Chang EY, Szallasi Z, Blumberg PM, Rivera J: Tyrosine phosphorylation of protein kinase C-δ in response to the activation of the high-affinity receptor for immunoglobulin E modifies its substrate recognition. Proc Natl Acad Sci USA 1995, 92:9112-9116.
33. 2, and are found in several signaling molecules, proteins containing PH domains are a potentially important class of PKC-binding proteins.
34. Konishi H, Kuroda S, Tanaka M, Matsuzaki H, Ono Y, Kameyama K, Haga T, Kikkawa U: Association of the pleckstrin homology domain of three types of RAC protein kinase C subspecies and βγ subunits of G proteins. Biochem Biophys Res Commun 1995, 216:526-534.
35. Newton AC: Seeing two domains. Curr Biol 1995, 5:973-976. This is a concise review of PKC lipid-binding domains.
36. 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. A model for protein kinase C conformational changes. J Biol Chem 1995, 270:19651-19658.
37. Ron D, Luo J, Mochly-Rosen D: C2 region-derived peptides inhibit translocation and function of β protein kinase C in vitro. J Biol Chem 1995, 270:24180-24187.
38. Pears C, Schaap D, Parker PJ: The regulatory domain of protein kinase C-ε restricts the catalytic domain specificity. Biochem J 1991, 276:257-260.
39. Zhang J, Wang L, Schwartz J, Bond RW, Bishop WR: Phosphorylation of Thr642 is an early event in the processing of newly synthesized protein kinase C β1 and is essential for its activation. J Biol Chem 1994, 269:19578-19584. PKCs with mutations in Thr642 that are not phosphorylatable at this residue partition into the Triton-insoluble fraction and attenuate phorbol ester mediated increases in gene expression. Thus, phosphorylation of Thr642 is required for proper PKC targeting. Alignments identify residues homologous to Thr642 in the carboxyl termini of other PKCs, indicating that this may be a general PKC regulatory motif.
40. Li W, Yu J-C, Shin D-Y, Pierce JH: Characterization of a protein kinase C-δ (PKC-δ) ATP binding mutant. An inactive enzyme that competitively inhibits wild type PKC-δ enzymatic activity. J Biol Chem 1995, 270:8311-8318.
41. Berra E, Diazmeco MT, Dominguez I, Municio MM, Sanz L, Lozano J, Chapkin RS, Moscat J: Protein kinase-C-ζ isoform is critical for mitogenic signal transduction. Cell 1993, 74:555-563.
42. Dutil EM, Keranen LM, DePaoli-Roach AA, Newton AC: In vivo regulation of protein kinase C by trans-phosphorylation followed by autophosphorylation. J Biol Chem 1994, 269:29359-29362.
43. Kahn SM, O'Driscoll KR, Jiang W, Borner C, Xu DB, Blackwood MA, Zhang Y, Nomoto K, Weinstein IB: Suppression of mitogenic activity by stable expression of the regulatory domain of PKCβ. Carcinogenesis 1994, 15:2919-2925.
44. Diaz-Meco MT, Lozano J, Municio MM, Berra E, Frutos S, Sanz L, Moscat J: Evidence for the in vitro and in vivo interaction of ras with protein kinase Cε. J Biol Chem 1994, 269:31706-31710.
45. Ahmad S, Safa AR, Glazer RI: Modulation of P-glycoprotein by protein kinase C α in a baculovirus expression system. Biochemistry 1994, 33:10313-10318.
46. Balboa MA, Firestein BL, Godson C, Bell KS, Insel PA: Protein kinase C-α mediates phospholipase D activation by nucleotides and phorbol ester in Madin-Darby canine kidney cells. J Biol Chem 1994, 269:10511-10516.
47. Godson C, Bell KS, Insel PA: Inhibition of expression of protein kinase-C-α by antisense cDNA inhibits phorbol ester-mediated arachidonate release. J Biol Chem 1993, 268:11946-11950.
48. Dean NM, McKay R, Condon TP, Bennett CF: Inhibition of protein kinase C-α expression in human A549 cells by antisense oligonucleotides inhibits induction of intercellular adhesion molecule 1 (ICAM-1) mRNA by phorbol esters. J Biol Chem 1994, 269:16416-16424.
49. Dean NM, McKay R: Inhibition of protein kinase C-α expression in mice after systemic administration of phosphorothioate antisense oligodeoxy-nucleotides. Proc Natl Acad Sci USA 1994, 91:11762-11766. Highly specific phosphorothioate antisense oligonucleotides were shown to decrease PKC levels in, and attenuate growth of, cultured cells. Because of the similarities among the PKCs and the complexities of analyzing functions in cells expressing more than one isozyme of PKC, antisense oligonucleotides potentially provide a powerful approach toward determining isozyme-specific inhibition.
50. Watanabe T, Ono Y, Taniyama Y, Hazama K, Igarashi K, Ogita K, Kikkawa U, Nishizuka Y: Cell division arrest induced by phorbol ester in CHO cells overexpressing protein kinase-C-δ subspecies. Proc Natl Acad Sci USA 1992, 89:10159-10163.
51. Mischak H, Goodnight J, Kolch W, Martiny-Baron G, Schaechtle C, Kazanietz MG, Blumberg PM, Pierce JH, Mushinsk JF: Overexpression of protein kinase C-δ and -ε in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity. J Biol Chem 1993, 268:6090-6096.
52. Yamaguchi K, Ogita K, Nakamura S, Nishizuka Y: The protein kinase C isoforms leading to MAP-kinase activation in CHO cells. Biochem Biophys Res Commun 1995, 210:639-647.
53. Borner C, Ueffing M, Jaken S, Parker PJ, Weinstein IB: Two closely related isoforms of protein kinase C produce reciprocal effects on the growth of rat fibroblasts. Possible molecular mechanisms. J Biol Chem 1995, 270:78-86.
54. Goldstein DR, Cacace AM, Weinstein IB: Overexpression of protein kinase C β1 in the SW480 colon cancer cell line causes growth suppression. Carcinogenesis 1995, 16:1121-1126.
55. Su ZZ, Duigou GJ, Fisher PB: Low-level β1 protein kinase C expression in cloned rat embryo fibroblast cells enhances transformation induced by the adenovirus type-5 E1A gene. Mol Carcinog 1991, 4:328-337.
56. Hsiao W, Housey GM, Johnson MD, Weinstein IB: Cells that overproduce protein kinase C are more susceptible to transformation by an activated H-ras oncogene. Mol Cell Biol 1989, 9:2641-2647.
57. Chapline C, Mousseau B, Ramsay K, Duddy S, Li Y, Kiley S, Jaken S: Identification of a major protein kinase C binding protein and substrate in rat embryo fibroblasts: decreased expression in transformed cells. J Biol Chem 1996, in press. The major PKC-binding protein/substrate in REF52 cells, clone 72, is down-modulated in transformed cells. Changes in PKC levels, PKC location and PKC substrates must all be considered as important components of PKC signaling pathways, in which changes contributing to transformation could occur.
58. Yang L, Glaser M: Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C. Biochemistry 1995, 34:1500-1506. Addition of PKC substrate peptides to mixed phospholipid vesicles causes PS to organize into discrete domains. PKC phosphorylation of substrate proteins directly correlates with co-organization of substrates and PS in these domains.