Casein kinase 2 associates with and phosphorylates Dishevelled
Casein kinase 2 associates with and phosphorylates Dishevelled
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DOI：
10.1093/emboj/16.11.3089
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发表时间：
1997-06
期刊：
影响因子：
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通讯作者：
K. Willert;M. Brink;A. Wodarz;H. Varmus;R. Nusse
中科院分区：
文献类型：
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作者：
K. Willert;M. Brink;A. Wodarz;H. Varmus;R. Nusse
果蝇Dheveled(Dsh)基因编码一种磷酸蛋白，其磷酸化状态在无翼刺激下被上调，这表明Dsh的磷酸化和负责这种磷酸化的激酶(S)是Wg信号通路中不可分割的一部分。我们发现，从胚胎和组织培养细胞中免疫沉淀的Dsh蛋白与体外磷酸化Dsh的激酶活性有关。纯化和测序表明，该蛋白与果蝇酪蛋白激酶2(CK2)同源。胰酶磷酸肽图谱显示，在体外和体内，相同的多肽都被CK2磷酸化，这表明CK2至少是一种磷酸化Dsh的酶。无翼受体Dfz2的过表达也刺激了Dsh的磷酸化，Dsh相关的激酶活性，以及CK2与Dsh的关联，从而表明CK2在Wg信号的转导中发挥了作用。
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.