Molecular organization of the uvomorulin-catenin complex.
Molecular organization of the uvomorulin-catenin complex.
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DOI：
10.1083/jcb.116.4.989
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发表时间：
1992-02
影响因子：
7.8
通讯作者：
Kemler, R
中科院分区：
文献类型：
--
作者：
Ozawa, M;Kemler, R
钙依赖性细胞粘附分子uvomorulin是钙粘蛋白基因家族的一员。它的胞质区域与结构上确定的蛋白质复合，称为α-，β-和γ-连环蛋白。在这里，我们表明，A-CAM（N-钙粘蛋白），这个基因家族的另一个成员，也与连环蛋白，这表明这种复合物的形成可能是一个普遍的特性的钙粘蛋白。对于uvomorulin，人们发现与连环蛋白的这种结合对于粘附功能至关重要，但人们对uvomorulin-连环蛋白复合物的分子组织知之甚少。使用生物化学分析的组合，我们表明，一个单一的复合物是由一个分子的uvomorulin，一个或两个分子的β-连环蛋白，和一个分子的α-连环蛋白。此外，β-连环蛋白似乎更直接地与uvomorulin相互作用。在脉冲追踪实验中，β-连环蛋白已经与135-kD的uvomorulin前体分子相关联，但是新合成的α-连环蛋白组装成复合物仅在蛋白内切加工的时间附近检测到。
The Ca(2+)-dependent cell adhesion molecule uvomorulin is a member of the cadherin gene family. Its cytoplasmic region complexes with structurally defined proteins termed alpha-, beta-, and gamma-catenins. Here we show that A-CAM (N-cadherin), another member of this gene family, also associates with catenins suggesting that this complex formation may be a general property of the cadherins. For uvomorulin it has been found that this association with catenins is of crucial importance for the adhesive function, but little is known about the molecular organization of the uvomorulin-catenin complex. Using a combination of biochemical analyses we show that a single complex is composed of one molecule of uvomorulin, one or two molecules of beta- catenin, and one molecule of alpha-catenin. Furthermore, beta-catenin seems to interact more directly with uvomorulin. In pulse-chase experiments beta-catenin is already associated with the 135-kD uvomorulin precursor molecule but the assembly of the newly synthesized alpha-catenin into the complex is only detected around the time of endoproteolytic processing.