Functional interaction of an axin homolog, conductin, with β-catenin, APC, and GSK3β
Functional interaction of an axin homolog, conductin, with β-catenin, APC, and GSK3β
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DOI：
10.1126/science.280.5363.596
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发表时间：
1998-04-24
期刊：
影响因子：
56.9
通讯作者：
Birchmeier, W
中科院分区：
文献类型：
--
作者：
Behrens, J;Jerchow, BA;Birchmeier, W
β-连环蛋白稳定性的调控在Wnt信号通路中至关重要。在此，发现蛋白传导蛋白（conductin）可与β-连环蛋白以及肿瘤抑制基因产物腺瘤性息肉病 coli（APC）形成复合物。传导蛋白诱导β-连环蛋白降解，而缺乏复合物形成能力的传导蛋白突变体则使β-连环蛋白稳定。含有传导蛋白结合结构域的APC片段也可阻断β-连环蛋白的降解。因此，传导蛋白是引导β-连环蛋白降解的多蛋白复合物的一个组分，且位于APC的下游。在非洲爪蟾胚胎中，传导蛋白干扰Wnt诱导的轴形成。
Control of stability of beta-catenin is central in the wnt signaling pathway. Here, the protein conductin was found to form a complex with both beta-catenin and the tumor suppressor gene product adenomatous polyposis coli (APC), Conductin induced beta-catenin degradation, whereas mutants of conductin that were deficient in complex formation stabilized beta-catenin. Fragments of APC that contained a conductin-binding domain also blocked beta-catenin degradation. Thus, conductin is a component of the multiprotein complex that directs beta-catenin to degradation and is located downstream of APC. In Xenopus embryos, conductin interfered with wnt-induced axis formation.