Domains of Axin and disheveled required for interaction and function in Wnt signaling
Domains of Axin and disheveled required for interaction and function in Wnt signaling
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DOI：
10.1006/bbrc.2000.3607
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发表时间：
2000-10-05
影响因子：
3.1
通讯作者：
Kitajewski, J
中科院分区：
文献类型：
--
作者：
Julius, MA;Schelbert, B;Kitajewski, J
disheveld通过与支架蛋白Axin相互作用，阻断β -连环蛋白对Wnt信号的降解。为了详细定义这种相互作用，我们对小鼠轴蛋白和散乱蛋白进行了突变和结合分析。Axin的DIX结构域对于与Disheveled的关联很重要，而Axin的另外两个区域（在残基1-168和600-810之间）仅被发现可以促进Axin与Disheveled的关联。我们发现Disheveled的DM结构域对于体内与轴蛋白的关联和Disheveled活性至关重要。Disheveled DIX结构域控制着Disheveled诱导细胞质β -连环蛋白积累的能力，而PDZ结构域对这一功能并不重要。(C) 2000年学术出版社。
Disheveled blocks the degradation of beta-catenin in response to Wnt signal by interacting with the scaffolding protein, Axin. To define this interaction in detail we undertook a mutational and binding analysis of the murine Axin and Disheveled proteins. The DIX domain of Axin was found to be important for association with Disheveled and two other regions of Axin (between residues 1-168 and 600-810) mere identified that can promote the association of Axin and Disheveled. We found that the DM domain of Disheveled is critical for association with Axin in vivo and for Disheveled activity. The Disheveled DIX domain controlled the ability of Disheveled to induce the accumulation of cytosolic beta-catenin whereas the PDZ domain was not essential to this function. (C) 2000 Academic Press.