Phosphorylation of CaBP1 and CaBP2 by protein kinase CK2

Journal of Biochemistry

Volumn 121, Issue 1, 1997, Pages 112-117

  Janson, Inger M ^a   Ek, Bo ^b   Ek, Pia ^a  

^a UPPSALA UNIVERSITY   (Sweden)

^b SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

Author keywords

CaBP1; CaBP2; Endoplasmic reticulum; Liver; Protein kinase CK2

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM BINDING PROTEIN; CASEIN KINASE II; PHOSPHORUS 32; PROTEIN KINASE; SERINE; SIGNAL PEPTIDE; THREONINE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; AUTORADIOGRAPHY; CARBOXY TERMINAL SEQUENCE; CATTLE; ENDOPLASMIC RETICULUM; ENZYME SUBSTRATE; LIVER MICROSOME; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN PHOSPHORYLATION; RAT; SEQUENCE ANALYSIS;

ANIMALIA; BOS TAURUS; BOVINAE; MAMMALIA; MURINAE;

EID: 0031032915     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021552     Document Type: Article

References (48)

1. Helenius, A., Marquardt, T., and Braakman, I. (1992) The endoplasmatic reticulum as a protein-folding compartment. Trends Cell. Biol. 2, 227-231
2. Freedman, R.B. (1992) Protein folding in vivo in Protein Folding (Creighton, T.E., ed.) pp. 455-539, W.H. Freeman and Co., New York
3. Gething, M.-J. and Sambrook, J. (1992) Protein folding in the cell. Nature 355, 33-45
4. Hwang, C., Sinskey, A., and Lodish, H. (1992) Oxidized redox state of glutathione in the endoplasmatic reticulum. Science 257, 1496-1502
5. Gaut, J.R. and Hendershot, L.M. (1993) The modification and assambly of proteins in the endoplasmic reticulum. Curr. Opin. Cell. Biol. 5, 589-595
6. Braakman, I., Helenius, J., and Helenius, A. (1992) Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature 356, 260-262
7. Clairmont, C.A., De Maio, A., and Hirschberg, C.B. (1992) Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to lumenal proteins including BiP (GRP 78) and GRP 94. J. Biol. Chem. 267, 3983-3990
8. Wickner, W.T. (1994) How ATP drives proteins across membranes. Science 208, 1197-1198
9. Rothman, J.E. (1989) Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59, 591-601
10. Gaut, J.R. and Hendershot, L.M. (1993) Mutation within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain. J. Biol. Chem. 268, 12691-12698
11. 2+-binding proteins and members of the thioredoxin super-family. J. Biol. Chem. 269, 1744-1749
12. Satoh, M., Nakai, A., Sokawa, Y., Hirayoshi, K., and Nagata, N. (1993) Modulation of the phosphorylation of glucose-regulated protein, GRP78, by transformation and inhibition of glucosylation. Exp. Cell Res. 205, 76-83
13. Wada, I., Rindress, D., Cameron, P.H., Ou, W.-J., James, J., Doherty, J.J., Louvard, D.D.L., Bell, A.W., Dignard, D., Thomas, D.Y., and Bergeron, J.J.M. (1991) SSRα and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J. Biol. Chem. 266, 19599-19610
14. Ou, W.-J., Thomas, D.Y., Bell, A.W., and Bergeron, J.J.M. (1992) Casein kinase II phosphorylation of signal sequence receptor α and the associated membrane chaperone calnexin. J. Biol. Chem. 267, 23789-23796
15. Cala, S.E., Ulbright, C., Kelley, J.S., and Jones, L.R. (1993) Purification of a 90-kDa protein (band VII) from cardiac sarco-plasmic reticulum. J. Biol. Chem. 268, 2969-2975
16. Schue, V., Green, G.A., Girardot, R., and Monteil, R. (1994) Hyperphosphorylation of calnexin, a chaperone protein, induced by Clostridium difficile cytotoxin. Biochem. Biophys. Res. Commun. 203, 22-28
17. Cala, S.E. and Jones, L.R. (1994) GRP94 resides within cardiac sarcoplasmic reticulum vesicles and is phosphorylated by casein kinase II. J. Biol. Chem. 269, 5926-5931
18. Quéméneur, E., Guthapfel, R., and Gueguen, P. (1994) A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase. J. Biol. Chem. 269, 5485-5488
19. Leustek, T., Toledo, H., Brot, N., and Wrissbach, H. (1991) Calcium-dependent autophosphorylation of the glucose-regulated protein, Grp78. Arch. Biochem. Biophys. 289, 256-261
20. Hendershot, L.M., Ting, J., and Lee, A.S. (1988) Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttanslational modifications in its binding function. Mol. Cell. Biol. 8, 4250-4256
21. Freedman, R.B., Hirst, T.R., and Tuite, M.F. (1994) Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19, 331-336
22. Meggio, P., Donella Deana, A., and Pinna, L.A. (1981) Endogenous phosphate acceptor proteins for rat liver cytosolic casein kinases. J. Biol. Chem. 256, 11958-11961
23. Pertoft, H. and Smedsröd, B. (1987) Cell Separation in Methods and Selected Applications (Pretlow, T.P. and Pretlow, T.P., eds.) Vol. 4, Academic Press, New York
24. Ljungström, O. and Ekman, P. (1977) Glucagon-induced phosphorylation of pyruvate kinase (type L). Biochem. Biophys. Res. Commun. 78, 1147-1155
25. Laemmli, U.K. (1970) Cleavage of structural proteins during assambly of the head of bacteriophage T4. Nature 227, 680-685
26. Roos, P.H. (1990) Analytical fractionation of microsomal cytochrome P-450 isoenzymes from rat liver by high-performance ion-exchange chromatography. J. Chromatogr. 521, 251-265
27. O'Farrel, P.H. (1975) High resolution two-dimensional electrophoresis. J. Biol. Chem. 250, 4007-4021
28. 32P in small volumes. Anal. Biochem. 63, 1-4
29. Rosenfeld, J., Capdevielle, J., Guillemot, J.C., and Ferrara, P. (1992) In-gel digestion of proteins for internal sequence analysis after one- or two-dimensional gel electrophoresis. Anal. Biochem. 203, 173-179
30. Huffman, H.J. and Celis, J.E. (1994) Cell Biology, a Laboratory Handbook pp. 309-312, Academic Press, New York
31. Hathaway, G.M., Lubben, T.H., and Traugh, J.A. (1980) Inhibition of casein kinase II by heparin. J. Biol. Chem. 255, 8038-8041
32. Meggio, F., Agostinis, P., and Pinna, L.A. (1985) Casein kinases and their protein substrates in rat liver cytosol: evidence for their participation in multimolecular systems. Biochim. Biophys. Acta 846, 248-256
33. Fuellekrug, J., Soennichsen, B., Wuensch, U., Arseven, K., Van Nguyen, P., Söling, H.D., and Mieskes, G. (1994) CaBP1, a calcium binding protein of the thioredoxin family, is a resident protein of the ER and not of the Intermediate compartment. J. Cell Sci. 107, 2719-2727
34. Van Nguyen, P., Rupp, K., Lampen, A., and Söling, H.-D. (1993) CaBP2 is a rat homolog of ERp72 with protein disulfide isomerase activity. Eur. J. Biochem. 213, 789-795
35. Shi, Y., Brown, E.D., and Walsh, C.T. (1994) Expression of recombinant human casein kinase II and recombinant heat shock protein 90 in Escherichia coli and their interactions. Proc. Natl. Acad. Sci. USA 91, 2767-2771
36. Chaudhuri, M.M., Tonin, P.N., Lewis, W.H., and Srinivasan, P.R. (1992) The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells. Biochem. J. 281, 645-650
37. Peter, F., Van Nguyen, P., and Söling, H.-D. (1992) Different sorting of Lys-Asp-Glu-Leu proteins in rat liver. J. Biol. Chem. 267, 10631-10637
38. Van Nguyen, P., Peter, F., and S̈ling, H.-D. (1989) Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. J. Biol. Chem. 264, 17494-17501
39. Mitev, V., Pauloin, A., and Houdebine, L.-M. (1994) Purification and characterization of two casein kinase type II isoenzymes from bovine gray matter. J. Neurochem. 63, 717-726
40. Ahn, N.G., Weiel, J.E., Chan, C.P., and Krebs, E.G. (1990) Identification of multiple epidermal growth factor-stimulated protein serine/threonine kinases from Swiss 3T3 cells. J. Biol. Chem. 265, 11487-11494
41. Elizarov, S.M. (1989) Application of fast protein liquid chromatography for the isolation of vertebrate casein kinase-1. J. Chromatogr. 477, 448-453
42. Rupp, K., Birnbach, U., Lundström, J., Van Nguyen P., and Söling, H.-D. (1994) Effects of CaBP2, the rat analog of ERp72, and of CaBPl on the refolding of denatured reduced proteins. J. Biol. Chem. 269, 2501-2507
43. Lundström-Ljung, J., Birnbach, U., Rupp, K., Söling, H.-D., and Holmgren, A. (1995) Two resident ER proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulphide isomerase. FEES Lett. 357, 305-308
44. Urade, R., Takenaka, Y., and Kito, M. (1993) Protein degradation by ERp72, from rat and mouse liver endoplasmic reticulum. J. Biol. Chem. 268, 22004-22009
45. Weisbart, R.H. (1992) An antibody that binds a neutrophil membrane protein, ERp72, primes human neutrophils for enhanced oxidative metabolism in response to formyl-methionyl-leucyl-phenylalanine. Implications for ERp72 in the signal transduction pathway for neutrophil priming. J. Immunol. 148, 3958-3963
46. Srinivasan, M., Lenny, N., and Green, M. (1993) Identification of genomic sequences that mediate the induction of the endoplasmic reticulum stress protein. DNA Cell. Biol. 12, 807-822
47. Kuznetsov, G., Chen, L.B., and Nigam, S.K. (1994) Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation. J. Biol. Chem. 269, 22990-22995
48. Lewis, M.J. and Pelham, H.R. (1992) Sequence of a second human KDEL receptor. J. Mol. Biol. 226, 913-916