PX-RICS-14-3-3zeta/theta 复合物将 N-钙黏蛋白-β-连环蛋白与动力蛋白-动力蛋白复合物结合，将其从内质网中输出。
The PX-RICS-14-3-3zeta/theta complex couples N-cadherin-beta-catenin with dynein-dynactin to mediate its export from the endoplasmic reticulum.
机构信息
Laboratory of Molecular and Genetic Information, Institute of Molecular and Cellular Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.
出版信息
J Biol Chem. 2010 May 21;285(21):16145-54. doi: 10.1074/jbc.M109.081315. Epub 2010 Mar 22.
We have recently shown that beta-catenin-facilitated export of cadherins from the endoplasmic reticulum requires PX-RICS, a beta-catenin-interacting GTPase-activating protein for Cdc42. Here we show that PX-RICS interacts with isoforms of 14-3-3 and couples the N-cadherin-beta-catenin complex to the microtubule-based molecular motor dynein-dynactin. Similar to knockdown of PX-RICS, knockdown of either 14-3-3zeta or - resulted in the disappearance of N-cadherin and beta-catenin from the cell-cell boundaries. Furthermore, we found that PX-RICS and 14-3-3zeta/ are present in a large multiprotein complex that contains dynein-dynactin components as well as N-cadherin and beta-catenin. Both RNAi- and dynamitin-mediated inhibition of dynein-dynactin function also led to the absence of N-cadherin and beta-catenin at the cell-cell contact sites. Our results suggest that the PX-RICS-14-3-3zeta/ complex links the N-cadherin-beta-catenin cargo with the dynein-dynactin motor and thereby mediates its endoplasmic reticulum export.
我们最近表明，β-连环蛋白促进钙黏蛋白从内质网输出需要 PX-RICS，这是一种β-连环蛋白相互作用的 GTP 酶激活蛋白，作用于 Cdc42。在这里，我们表明 PX-RICS 与 14-3-3 的同工型相互作用，并将 N-钙黏蛋白-β-连环蛋白复合物与基于微管的分子马达动力蛋白 dynein-dynactin 偶联。类似于 PX-RICS 的敲低，敲低 14-3-3zeta 或 - 导致 N-钙黏蛋白和 β-连环蛋白从细胞-细胞边界消失。此外，我们发现 PX-RICS 和 14-3-3zeta/- 存在于一个包含动力蛋白 dynactin 成分以及 N-钙黏蛋白和 β-连环蛋白的大型多蛋白复合物中。RNAi 和 dynamitin 介导的对 dynein-dynactin 功能的抑制也导致 N-钙黏蛋白和 β-连环蛋白在细胞-细胞接触部位缺失。我们的结果表明，PX-RICS-14-3-3zeta/ 复合物将 N-钙黏蛋白-β-连环蛋白货物与动力蛋白 dynactin 马达连接，并由此介导其内质网输出。
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