Structural basis of interaction between protein tyrosine phosphatase PCP-2 and β-catenin

被引：0
|
作者：
Yaqin He
Hexin Yan
Hui Dong
Peng Zhang
Liang Tang
Xiuhua Qiu
Mengchao Wu
Hongyang Wang
机构：
[1] Eastern Hepatobiliary Surgery Hospital,International Co
[2] Second Military Medical University,operation Laboratory on Signal Transduction
来源：
Science in China Series C: Life Sciences | 2005年 / 48卷 / 2期
关键词：
PCP-2; β-catenin; protein tyrosine phosphatase; interaction;
D O I：
10.1007/BF02879669
中图分类号：
学科分类号：
摘要：
PCP-2 is a member of receptor-like protein tyrosine phosphatase of the MAM domain family. To investigate which part of PCP-2 was involved in its interaction with β-catenin, we constructed various deletion mutants of PCP-2. These PCP-2 mutants and wild-type PCP-2 were co-transfected into BHK-21 cells with β-catenin individually. Anin vivo binding assay revealed that the expression of wild-type PCP-2, PCP-2 ΔC1C2 (deleted PCP-2 without both PTP domains) and PCP-2 ΔC2 (deleted PCP-2 without the second PTP domain) could be immunoprecipitated by anti-catenin antibody in every co-transfection, but PCP-2 EXT (deleted PCP-2 without the juxtamembrane region and both PTP domains) was missing, which implied that PCP-2 and β-catenin could associate directly and the juxtamembrane region in PCP-2 was sufficient for the process.
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页码：163 / 167
页数：4
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