p120-Catenin Is a Key Component of the Cadherin-γ-Secretase Supercomplex
p120-Catenin Is a Key Component of the Cadherin-γ-Secretase Supercomplex
复制标题
DOI：
10.1091/mbc.e08-04-0394
复制
发表时间：
2008-10-01
影响因子：
3.3
通讯作者：
Troyanovsky, Sergey M.
中科院分区：
文献类型：
--
作者：
Kiss, Alexi;Troyanovsky, Regina B.;Troyanovsky, Sergey M.
在这项工作中，我们显示了一些以前未知的功能p120-连环蛋白在钙粘蛋白-连环蛋白复合物，是我们的理解钙粘蛋白为基础的粘附和信号传导的关键。我们发现，在人类上皮A-431细胞中，几乎所有的p120分子都与位于细胞表面的E-cadherin-catenin复合物进行高亲和力的相互作用。p120在与钙粘蛋白的复合物中位于α-连环蛋白附近。这些发现表明p120和α-连环蛋白之间的功能合作，在钙粘蛋白为基础的粘附。相反，低水平的无钙粘蛋白的p120分子可以促进p120依赖性信号传导。最后，我们提出了令人信服的证据表明，p120是一个关键的连接器水泥E-钙粘蛋白-连环蛋白复合物与跨膜蛋白酶γ-分泌酶。这种超复合物的细胞-细胞接触位置使其成为传导依赖于γ-分泌酶蛋白水解活性的不同信号的重要候选者。
In this work, we show several previously unknown features of p120-catenin in a cadherin-catenin complex that are critical for our understanding of cadherin-based adhesion and signaling. We show that in human epithelial A-431 cells, nearly all p120 molecules engage in high-affinity interaction with E-cadherin-catenin complexes located at the cellular surface. p120 is positioned in proximity to alpha-catenin in the complex with cadherin. These findings suggest a functional cooperation between p120 and alpha-catenin in cadherin-based adhesion. A low level of cadherin-free p120 molecules, in contrast, could facilitate p120-dependent signaling. Finally, we present compelling evidence that p120 is a key linker cementing the E-cadherin-catenin complex with the transmembrane protease gamma-secretase. The cell-cell contact location of this supercomplex makes it an important candidate for conducting different signals that rely on gamma-secretase proteolytic activity.