Hiscox S, Jiang W G
Metastasis Research Group, Department of Surgery, University of Wales College of Medicine, Heath Park, Cardiff CF4 4XN, UK.
Int J Oncol. 1998 Nov;13(5):1077-80. doi: 10.3892/ijo.13.5.1077.
Protein tyrosine phosphorylation and dephosphorylation is regulated by the action of protein tyrosine kinases (PTK) and phosphatases (PTP) respectively. The receptor type phosphatase, PTPmu, is located at the cell surface where it may function to regulate the phosphoryl status of members of the cadherin adhesion complex and thus cadherin function. We have investigated the association of PTPmu with E-cadherin and catenin molecules in human tumour cells and report that PTPmu; is associated with E-cadherin and alpha and beta-catenin in E-cadherin-positive cell lines. However, no association between PTPmu and catenin members could be detected in E-cadherin negative cells. These observations suggest that the association of PTPmu with catenin molecules may occur via E-cadherin rather than a direct interaction.
蛋白质酪氨酸磷酸化和去磷酸化分别由蛋白质酪氨酸激酶(PTK)和磷酸酶(PTP)的作用来调节。受体型磷酸酶PTPmu位于细胞表面,在那里它可能发挥作用来调节钙黏蛋白黏附复合体成员的磷酸化状态,从而影响钙黏蛋白的功能。我们研究了PTPmu与人肿瘤细胞中E-钙黏蛋白和连环蛋白分子的关联,并报告PTPmu;在E-钙黏蛋白阳性细胞系中与E-钙黏蛋白以及α和β连环蛋白相关联。然而,在E-钙黏蛋白阴性细胞中未检测到PTPmu与连环蛋白成员之间的关联。这些观察结果表明,PTPmu与连环蛋白分子的关联可能是通过E-钙黏蛋白发生的,而不是直接相互作用。