Serine phosphorylation-regulated ubiquitination and degradation of beta-catenin
Serine phosphorylation-regulated ubiquitination and degradation of beta-catenin
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DOI：
10.1074/jbc.272.40.24735
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发表时间：
1997-10-03
影响因子：
4.8
通讯作者：
Byers, SW
中科院分区：
文献类型：
--
作者：
Orford, K;Crockett, C;Byers, SW
我们发现β -连环蛋白被蛋白酶体泛素化和降解，并且β -连环蛋白的稳定性受到不依赖于二酰基甘油的蛋白激酶c样激酶活性的调节，这是β -连环蛋白泛素化所必需的。我们还定义了在β -连环蛋白和nf - κ B调节蛋白I κ B α中发现的一个姐妹氨基酸序列，该序列在磷酸化后，针对这两种蛋白进行泛素化。泛素化靶向序列中单个丝氨酸的突变可阻止β -连环蛋白的泛素化。β -连环蛋白泛素化靶向序列的突变可能致癌。
Several lines of evidence suggest that accumulation of cytoplasmic beta-catenin transduces an oncogenic signal We show that beta-catenin is ubiquitinated and degraded by the proteosome and that beta-catenin stability is regulated by a diacylglycerol-independent protein kinase C-like kinase activity, which is required for beta-catenin ubiquitination. We also define a sis-amino acid sequence found in both beta-catenin and the NF-kappa B regulatory protein I kappa B alpha, which, upon phosphorylation, targets both proteins for ubiquitination. Mutation of a single serine within the ubiquitination targeting sequence prevents ubiquitination of beta-catenin. Mutations within the ubiquitination targeting sequence of beta-catenin may be oncogenic.