Src promotes PKCδ degradation

Cell Growth and Differentiation

Volumn 10, Issue 4, 1999, Pages 231-241

  Blake, Robert A ^a   Garcia Paramio, Pilar ^b   Parker, Peter J ^b   Courtneidge, Sara A ^a  

^a SUGEN INC   (United States)

^b IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PLATELET DERIVED GROWTH FACTOR BB; PROTEIN KINASE C; BROXURIDINE; CYCLOHEXIMIDE; ISOENZYME; PLATELET DERIVED GROWTH FACTOR; PRKCD PROTEIN, MOUSE; PROTEIN KINASE C DELTA; PROTEIN SYNTHESIS INHIBITOR; PROTEIN TYROSINE KINASE;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DNA SYNTHESIS; GENE MAPPING; MITOGENESIS; NONHUMAN; ONCOGENE SRC; PRIORITY JOURNAL; PROTEIN DEGRADATION; SIGNAL TRANSDUCTION; ANIMAL; CELL CYCLE; CELL STRAIN 3T3; DRUG ANTAGONISM; GENETIC TRANSFECTION; METABOLISM; MICROINJECTION; MOUSE; MUTAGENESIS; NORTHERN BLOTTING; PHOSPHORYLATION; PHYSIOLOGY; SERODIAGNOSIS; TIME;

3T3 CELLS; ANIMALS; BLOTTING, NORTHERN; BROMODEOXYURIDINE; CELL CYCLE; CYCLOHEXIMIDE; ISOENZYMES; MICE; MICROINJECTIONS; MUTAGENESIS; PHOSPHORYLATION; PLATELET-DERIVED GROWTH FACTOR; PRECIPITIN TESTS; PROTEIN KINASE C; PROTEIN KINASE C-DELTA; PROTEIN SYNTHESIS INHIBITORS; SIGNAL TRANSDUCTION; SRC-FAMILY KINASES; TIME FACTORS; TRANSFECTION;

EID: 0032587890     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (64)

1. Ralston, R., and Bishop, J. M. The product of the protooncogene c-src is modified during the cellular response to platelet-derived growth factor. Proc. Natl. Acad. Sci. USA, 82: 7845-7849, 1985.
2. Kypta, R. M., Goldberg, Y., Ulug, E. T., and Courtneidge, S. A. Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell, 62: 481-492, 1990.
3. Twamley-Stein, G. M., Pepperkok, R., Ansorge, W., and Courtneidge, S. A. The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells. Proc. Natl. Acad. Sci. USA, 90: 7696-7700, 1993.
4. Erpel, T., Alonso, G., Roche, S., and Courtneidge, S. A. The Src SH3 domain is required for DNA synthesis induced by platelet-derived growth factor and epidermal growth factor. J. Biol. Chem., 277: 16807-16812, 1996.
5. Broome, M. A., and Hunter, T. Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling. J. Biol. Chem., 271: 16798-16806, 1996.
6. Li, W., Yu, J. C., Michieli, P., Beeler, J. F., Ellmore, N., Heidaran, M. A., and Pierce, J. H. Stimulation of the platelet-derived growth factor β receptor signaling pathway activates protein kinase C-δ. Mol. Cell. Biol., 14: 6727-6735, 1994.
7. Hansen, K., Johnell, M., Siegbahn, A., Rorsman, C., Engstrom, U., Wernstedt, C., Heldin, C. H., and Ronnstrand, L. Mutation of a Src phosphorylation site in the PDGF β-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis. EMBO J., 75: 5299-5313, 1996.
8. McGlade, J., Cheng, A., Pelicci, G., Pelicci, P. G., and Pawson, T. She proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases. Proc. Natl. Acad. Sci. USA, 89: 8869-8873, 1992.
9. Jones, D. A., and Benjamin, C. W. Phosphotylation of growth factor receptor binding protein-2 by pp60c-src tyrosine kinase. Arch. Biochem. Biophys., 337: 143-148, 1997.
10. Jayaraman, T., Ondrias, K., Ondriasova, E., and Marks, A. R. Regulation of the inositol 1,4,5-trisphosphate receptor by tyrosine phosphorylation. Science (Washington DC), 272: 1492-1494, 1996.
11. Otsu, M., Hiles, I., Gout, I., Fry, M. J., Ruiz-Larrea, F., Panayotou, G., Thompson, A., Dhand, R., Hsuan, J., and Totty, N. Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/ pp60c-src complexes, and PI3-kinase. Cell, 65: 91-104, 1991.
12. Roche, S., Dhand, R., Waterfield, M. D., and Courtneidge, S. A. The catalytic subunit of phosphatidylinositol 3-kinase is a substrate for the activated platelet-derived growth factor receptor, but not for middle-T antigen-pp60c-src complexes. Biochem. J., 301: 703-711, 1994.
13. Gallo, R., Provenzano, C., Carbone, R., Di Fiore, P. P., Castellani, L., Falcone, G., and Alema, S. Regulation of the tyrosine kinase substrate Eps8 expression by growth factors, v-Src and terminal differentiation. Oncogene, 15: 1929-1936, 1997.
14. Gschwendt, M., Kielbassa, K., Kittstein, W., and Marks, F. Tyrosine phosphorylation and stimulation of protein kinase C δ from porcine spleen by src in vitro. Dependence on the activated state of protein kinase C δ. FEBS Lett., 347: 85-89, 1994.
15. Li, W., Mischak, H., Yu, J. C., Wang, L. M., Mushinski, J. F., Heidaran, M. A., and Pierce, J. H. Tyrosine phosphorylation of protein kinase C-δ in response to its activation. J. Biol. Chem., 269: 2349-2352, 1994.
16. Haleem-Smith, H., Chang, E. Y., Szallasi, Z., Blumberg, P. M., and 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, 92: 9112-9116, 1995.
17. Denning, M. F., Dlugosz, A. A., Howett, M. K., and Yuspa, S. H. Expression of an oncogenic rasHa gene in murine keratinocytes induces tyrosine phosphorylation and reduced activity of protein kinase C δ. J. Biol. Chem., 268: 26079-26081, 1993.
18. Zang, Q., Lu, Z., Curto, M., Barile, N., Shalloway, D., and Foster, D. A. Association between v-Src and protein kinase C δ in v-Src-transformed fibroblasts. J. Biol. Chem., 272: 13275-13280, 1997.
19. Leng, L., Du, B., Consigli, S., and McCaffrey, T. A. Translocation of protein kinase C-δ by PDGF in cultured vascular smooth muscle cells: inhibition by TGF-β 1. Artery, 22: 140-154, 1996.
20. Olivier, A. R., and Parker, P. J. 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., 269: 2758-2763, 1994.
21. Li, W., Michieli, P., Alimandi, M., Lorenzi, M. V., Wu, Y., Wang, L. H., Heidaran, M. A., and Pierce, J. H. Expression of an ATP binding mutant of PKC-δ inhibits Sis-induced transformation of NIH3T3 cells. Oncogene, 13: 731-737, 1996.
22. Watanabe, T., Ono, Y., Taniyama, Y., Hazama, K., Igarashi, K., Ogita, K., Kikkawa, U., and Nishizuka, Y. Cell division arrest induced by phorbol ester in CHO cells overexpressing protein kinase C-δ subspecies. Proc. Natl. Acad. Sci. USA, 89: 10159-10163, 1992.
23. Mischak, H., Goodnight, J. A., Kolch, W., Martiny-Baran, G., Schaechtle, C., Kazanietz, M. G., Blumberg, P. M., Pierce, J. H., and Mushinski, J. F. Overexpression of protein kinase C-δ and -ε in NIH 3T3 cells induces opposite effects or growth, morphology, anchorage dependence, and tumorigenicity. J. Biol. Chem., 268: 6090-6096, 1993.
24. Mishima, K., Ohno, S., Shitara, N., Yamaoka, K., and Suzuki, K. Opposite effects of the overexpression of protein kinase C γ and δ on the growth properties of human glioma cell line U251 MG. Biochem. Biophys. Res. Commun., 201: 363-372, 1994.
25. Stabel, S., Rodriguez-Pena, A., Young, S., Rozengurt, E., and Parker, P. J. Quantitation of protein kinase C by immunoblot: expression in different cell lines and response to phorbol esters. J. Cell. Physiol., 130: 111-117, 1987.
26. Young, S., Parker, P. J., Ullrich, A., and Stabel, S. Down-regulation of protein kinase C is due to an increased rate of degradation. Biochem. J., 244: 775-779, 1987.
27. Chen, C. C. Protein kinase C α, δ, ε and ζ in C6 glioma cells. TPA induces translocation and down-regulation of conventional and new PKC isoforms but not atypical PKC ζ. FEBS Lett., 332: 169-173, 1993.
28. Chen, C. C., Cheng, C. S., Chang, J., and Huang, H. C. Differential correlation between translocation and down-regulation of conventional and new protein kinase C isozymes in C6 glioma cells. J. Neurochem., 64: 818-824, 1995.
29. Prouty, S. M., Hanson, K. D., Boyle, A. L., Brown, J. R., Shichiri, M., Follansbee, M. R., Kang, W., and Sedivy, J. M. A cell culture model system for genetic analyses of the cell cycle by targeted homologous recombination. Oncogene, 8: 899-907, 1993.
30. Hochstrasser, M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol., 7: 215-223, 1995.
31. Murakami, Y., Matsufuji, S., Kameji, T., Hayashi, S., Igarashi, K., Tamura, T., Tanaka, K., and Ichihara, A. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature (Lond.), 360: 597-599, 1992.
32. Yu, C. L., and Burakoff, S. J. Involvement of proteasomes in regulating Jak-STAT pathways upon interteukin-2 stimulation. J. Biol. Chem., 272: 14017-14020, 1997.
33. Dick, L. R., Cruikshank, A. A., Destree, A. T., Grenier, L., McCormack, T. A., Melandri, F. D., Nunes, S. L., Palombella, V. J., Parent, L. A., Plamondon, L., and Stein, R. L. Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. J. Biol. Chem., 272: 162-188, 1997.
34. Lee, H. W., Smith, L., Pettit, G. R., Vinitsky, A., and Smith, J. B. Ubiquitination of protein kinase C-α and degradation by the proteasome. J. Biol. Chem., 271: 20973-20976, 1996.
35. Wiertz, E. J., Jones, T. R., Sun, L., Bogyo, M., Geuze, H. J., and Ploegh, H. L. The human cytomegatovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell, 84: 769-779, 1996.
36. Griscavage, J. M., Wilk, S., and Ignarro, L. J. Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-κ B. Proc. Natl. Acad. Sci. USA, 93: 3308-3312, 1996.
37. Hanke, J. H., Gardner, J. P., Dow, R. L., Changelian, P. S., Brissette, W. H., Weringer, E. J., Pollok, B. A., and Connelly, P. A. Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck-and FynT-dependent T cell activation. J. Biol. Chem., 271: 695-701, 1996.
38. Szallasi, Z., Denning, M. F., Chang, E. Y., Rivera, J., Yuspa, S. H., Lehel, C., Olah, Z., Anderson, W. B., and Blumberg, P. M. Development of a rapid approach to identification of tyrosine phosphorylation sites: application to PKC δ phosphorylated upon activation of the high affinity receptor for IgE in rat basophilic leukemia cells. Biochem. Biophys. Res. Commun., 214: 888-894, 1995.
39. Li, W., Chen, X. H., Kelley, C. A., Alimandi, M., Zhang, J., Chen, Q., Bottaro, D. P., and Pierce, J. H. Identification of tyrosine 187 as a protein kinase C-δ phosphorylation site. J. Biol. Chem., 271: 26404-26409, 1996.
40. 2. Proc. Natl. Acad. Sci. USA, 94: 11233-11237, 1997.
41. Kemp, B. E., and Pearson, R. B. Design and use of peptide substrates for protein kinases. Methods Enzymol., 200: 121-134, 1991.
42. Songyang, Z., Carraway, K. L. R., Eck, M. J., Harrison, S. C., Feldman, R. A., Mohammadi, M., Schlessinger, J., Hubbard, S. R., Smith, D. P., Eng, C., Lorenzo, M. J., Ponder, B. A. J., Mayer, B. J., and Cantley, L. C. Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature (Lond.), 373: 536-539, 1995.
43. Soltoff, S. P., and Toker, A. Carbachol, substance P, and phorbol ester promote the tyrosine phosphorylation of protein kinase C δ in salivary gland epithelial cells. J. Biol. Chem., 270: 13490-13495, 1995.
44. Lu, Z., Hornia, A., Jiang, Y. W., Zang, Q., Ohno, S., and Foster, D. A. Tumor promotion by depleting cells of protein kinase C δ. Mol. Cell. Biol., 17: 3418-3428, 1997.
45. Garcia-Paramio, P., Cabrerizo, Y., Bomancin, F., and Parker, P. J. The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation. Biochem. J., 333: 631-636, 1998.
46. Olivier, A. R., Hansra, G., Pettitt, T. R., Wakelam, M. J., and Parker, P. J. The co-mitogenic combination of transforming growth factor β 1 and bombesin protects protein kinase C-δ from late-phase down-regulation, despite synergy in diacylglycerol accumulation. Biochem. J., 318: 519-525, 1996.
47. Shih, N. Y., and Floyd-Smith, G. Protein kinase C-δ mRNA is down-regulated transcriptionally and post-transcriptionally by 12-O-tetradecanoylphorbol-13-acetate. J. Biol. Chem., 271: 16040-16046, 1996.
48. Lu, Z., Liu, D., Hornia, A., Devonish, W., Pagano, M., and Foster, D. A. Activation of protein kinase C triggers its ubiquitination and degradation. Mol. Cell. Biol., 18: 839-845, 1998.
49. Cohen, G. M. Caspases: the executioners of apoptosis. Biochem. J., 326: 1-16, 1997.
50. Lewis, L. A., Chung, C. D., Chen, J., Parnes, J. R., Moran, M., Patel, V. P., and Miceli, M. C. The Lck SH2 phosphotyrosine binding site is critical for efficient TCR-induced processive tyrosine phosphorylation of the ζ-chain and IL-2 production. J. Immunol., 159: 2292-2300, 1997.
51. Mayer, B. J., Hirai, H., and Sakai, R. Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. Curr. Biol., 5: 296-305, 1995.
52. Songyang, Z., Shoelson, S. E., Chaudhuri, M., Gish, G., Pawson, T., Haser, W. G., King, F., Roberts, T., Ratnofsky, S., and Lechleider, R. J. SH2 domains recognize specific phosphopeptide sequences. Cell, 72: 767-778, 1993.
53. Le Good, J. A., Ziegler, W. H., Parekh, D. B., Alessi, D. R., Cohen, P., and Parker, P. J. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science (Washington DC), 281: 2042-2045, 1998.
54. Cazaubon, S. M., and Parker, P. J. Identification of the phosphorylated region responsible for the permissive activation of protein kinase C. J. Biol. Chem., 268: 17559-17563, 1993.
55. Cazaubon, S., Bornancin, F., and Parker, P. J. Threonine-497 is a critical site for permissive activation of protein kinase C α. Biochem. J., 301: 443-448, 1994.
56. Bornancin, F., and Parker, P. J. Phosphorylation of protein kinase C-α on serine 657 controls the accumulation of active enzyme and contributes to its phosphalase-resistant state. J. Biol. Chem., 272: 3544-3549, 1997.
57. Herget, T., Oehrlein, S. A., Pappin, D. J., Rozengurt, E., and Parker, P. J. The myristoylated alanine-rich C-kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase C. Eur. J. Biochem., 233: 448-457, 1995.
58. Owen, P. J., Johnson, G. D., and Lord, J. M. Protein kinase C-δ associates with vimentin intermediate filaments in differentiated HL60 cells. Exp. Cell Res., 225: 366-373, 1996.
59. Kielbassa, K., Muller, H. J., Meyer, H. E., Marks, F., and Gschwendt, M. Protein kinase C δ-specific phosphorylation of the elongation factor eEF-α and an eEF-1 α peptide at threonine 431. J. Biol. Chem., 270: 6156-6162, 1995.
60. Garrone, B., Kedar, P., Elarova, I., Lavin, M., and Watters, D. Approaches to determine the specific role of the δ isoform of protein kinase C. J. Biochem. Biophys. Methods, 36: 51-61, 1997.
61. Murray, J. W., Edmonds, B. T., Liu, G., and Condeelis, J. Bundling of actin filaments by elongation factor 1 α inhibits polymerization at filament ends. J. Cell Biol., 135: 1309-1321, 1996.
62. Shiina, N., Gotoh, Y., Kubomura, N., Iwamatsu, A., and Nishida, E. Microtubule severing by elongation factor 1 α. Science (Washington DC), 266: 282-285, 1994.
63. Fumagalli, S., Totty, N. F., Hsuan, J. J., and Courtneidge, S. A. A target for Src in mitosis. Nature (Lond.), 368: 871-874, 1994.
64. Blake, R. A., Schieven, G. L., and Watson, S. P. Collagen stimulates tyrosine phosphorylation of phospholipase C-γ 2 but not phospholipase C-γ 1 in human platelets. FEBS Lett., 353: 212-216, 1994.