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Casein kinase 2 associates with and phosphorylates Dishevelled
Author(s) -
Willert Karl,
Brink Marcel,
Wodarz Andreas,
Varmus Harold,
Nusse Roel
Publication year - 1997
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/16.11.3089
Subject(s) - biology , casein kinase 1 , dishevelled , casein kinase 2 , phosphorylation , protein kinase a , casein , microbiology and biotechnology , biochemistry , signal transduction , mitogen activated protein kinase kinase , wnt signaling pathway , frizzled
The dishevelled ( dsh ) gene of Drosophila melanogaster encodes a phosphoprotein whose phosphorylation state is elevated by Wingless stimulation, suggesting that the phosphorylation of Dsh and the kinase(s) responsible for this phosphorylation are integral parts of the Wg signaling pathway. We found that immunoprecipitated Dsh protein from embryos and from cells in tissue culture is associated with a kinase activity that phosphorylates Dsh in vitro . Purification and peptide sequencing of a 38 kDa protein co‐purifying with this kinase activity showed it to be identical to Drosophila Casein Kinase 2 (CK2). Tryptic phosphopeptide mapping indicates that identical peptides are phosphorylated by CK2 in vitro and in vivo , suggesting that CK2 is at least one of the kinases that phosphorylates Dsh. Overexpression of Dfz2 , a Wingless receptor, also stimulated phosphorylation of Dsh, Dsh‐associated kinase activity, and association of CK2 with Dsh, thus suggesting a role for CK2 in the transduction of the Wg signal.