Casein kinase 2 associates with and phosphorylates dishevelled

EMBO Journal

Volumn 16, Issue 11, 1997, Pages 3089-3096

  Willert, Karl ^a,b   Brink, Marcel ^a   Wodarz, Andreas ^a   Varmus, Harold ^c   Nusse, Roel ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Casein kinase 2; Dishevelled; Frizzled; Wingless; Wnt

Indexed keywords

CASEIN KINASE II; PHOSPHOPROTEIN; PHOSPHOTRANSFERASE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; GENE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; CASEIN KINASE II; CELLS, CULTURED; DROSOPHILA; DROSOPHILA PROTEINS; FRIZZLED RECEPTORS; INSECT PROTEINS; PEPTIDE MAPPING; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN-SERINE-THREONINE KINASES; PROTO-ONCOGENE PROTEINS; RECEPTORS, CELL SURFACE; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, NEUROTRANSMITTER; RECOMBINANT PROTEINS;

EID: 0030973456     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.11.3089     Document Type: Article

References (28)

1. Allende, J.E. and Allende, C.C. (1995) Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J., 9, 313-23.
2. Bhanot, P., Brink, M., Harryman Samos, C., Hsieh, J.-C., Wang, Y., Macke, J.P., Andrew, D., Nathans, J. and Nusse, R. (1996) A new member of the frizzled family from Drosophila functions as a Wingless receptor. Nature, 382, 225-230.
3. Bidwai, A.P., Hanna, D.E. and Glover, C.V. (1992) Purification and characterization of casein kinase II (CKII) from delta cka1 delta cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits. The free catalytic subunit of casein kinase II is not toxic in vivo. J. Biol. Chem., 267, 18790-18796.
4. Boyle, W.J., van der Geer, P. and Hunter, T. (1991) Phosphopeptide Mapping and Phosphoamino Acid Analysis by Two-Dimensional Separation on Thin-Layer Cellulose Plates. Methods Enzymol., 201, 110-149.
5. Dahmus, G.K., Glover, C.V.C., Brutlag, D.L. and Dahmus, M.E. (1984) Similarities in structure and function of calf thymus and Drosophila Casein Kinase II. J. Biol. Chem., 259, 9001-9006.
6. Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M. and MacKinnon, R. (1996) Crystal structure of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell, 85, 1067-1076.
7. Giulian, G.G., Moss, R.L. and Greaser, M. (1983) Improved methodology for analysis and quantitation of proteins on one-dimensional silver-stained slab gels. Anal. Biochem., 129, 277-287.
8. Issinger, O.G. (1993) Casein kinases: pleiotropic mediators of cellular regulation. Pharmacol. Ther., 59, 1-30.
9. Klingensmith, J. and Nusse, R. (1994) Signaling by wingless in Drosophila. Dev. Biol., 166, 396-414.
10. Klingensmith, J., Nusse, R. and Perrimon, N. (1994) The Drosophila segment polarity gene dishevelled encodes a novel protein required for response to the wingless signal. Genes Dev., 8, 118-130.
11. Lindsley, D.L. and Zimm, G.G. (1992) The Genome of Drosophila melanogaster. Academic Press, San Diego, CA.
12. Luo, K., Hurley, T.R. and Sefton, B.M. (1991) Cyanogen bromide cleavage and proteolytic peptide mapping of proteins immobilized to membranes. Methods Enzymol., 201, 149-152.
13. Marshak, D.R. and Carroll, D. (1991) Synthetic peptide substrates for Casein Kinase II. Methods Enzymol., 201, 134-156.
14. McElhinny, J.A., Trushin, S.A., Bren, G.D., Nicholas, C. and Paya, C.V. (1996) Casein Kinase II phosphorylates IκBα at S-283, S-289, S-293, and T-291 and is required for its degradation. Mol. Cell Biol., 16, 899-906.
15. Morais Cabral, J.H., Petosa, C., Sutcliffe, M.J., Raza, S., Byron, O., Poy, F., Marfatia, S.M., Chishti, A.H. and Liddington, R.C. (1996) Crystal structure of a PDZ domain. Nature, 382, 649-652.
16. Muslin, A.J., Tanner, J.W., Allen, P.M. and Shaw, A.S. (1996) Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell. 84, 889-897.
17. Nusse, R. and Varmus, H.E. (1992) Wnt genes. Cell, 69, 1073-1087.
18. Pawson, T. (1995) Protein modules and signalling networks. Nature, 373, 573-580.
19. Peifer, M. (1993) The product of the Drosophila segment polarity gene armadillo is part of a multi-protein complex resembling the vertebrate adherens junction. J. Cell Sci. 105, 993-1000.
20. Perrimon, N. (1994) The genetic basis of patterned boldness in Drosophila. Cell, 76, 781-784.
21. Ponting, C.P. (1995) DHR domains in syntrophins, neuronal no synthases and other intracellular proteins. Trends Biol. Sci., 20, 102-103.
22. Ponting, C.P. (1996) Pleckstrin's repeat performance: a novel repeat in G-protein signaling? Trends Biol. Sci., 21, 245-246.
23. Rihs, H.-P., Jans, D.A., Hua, F. and Peters, R. (1991) The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J., 10, 633-639.
24. Saxema, A., Padmanabha, R. and Glover, C.V.C. (1987) Isolation and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster Casein Kinase II. Mol. Cell. Biol. 7, 3409-3417.
25. Songyang, Z. et al (1996) A structural basis for substrate specificities of protein ser/thr kinases: primary sequence preference of casein kinase I and II, phosphorylase kinase, calmodulin-dependent kinase, CDK5, and Erk1. Mol. Cell. Biol., 16, 6486-6493.
26. Sussman, D.J., Klingensmith, J., Salinas, P. Adams, P.S., Nusse, R. and Perrimon, N. (1994) Isolation and characterization of a mouse homolog of the Drosophila segment polarity gene dishevelled. Dev. Biol., 166, 73-86.
27. van Leeuwen, F., Harryman Samos, C. and Nusse, R. (1994) Biological activity of soluble wingless protein in cultured Drosophila imaginal disc cells. Nature, 368, 342-344.
28. Yanagawa, S., van Leeuwen, F., Wodarz, A., Klingensmith, J. and Nusse, R. (1995) The Dishevelled protein is modified by Wingless signaling in Drosophila. Genes Dev., 9, 1087-1097.