%0 Journal Article
%T Structural basis of interaction between protein tyrosine phosphatase PCP-2 and β-catenin
%A HE Yaqin
%A YAN Hexin
%A DONG Hui
%A ZHANG Peng
%A TANG Liang
%A QIU Xiuhua
%A WU Mengchao
%A WANG Hongyang
%A <br>
%J 中国科学C辑(英文版)
%D 2005
%I Springer
%X 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.
%K PCP-2
%K β
%K -catenin
%K protein tyrosine phosphatase
%K interaction<br>
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=180CF3A72E750F3261A8A60EDC957784&aid=48AF7E2B804FADC7E9F76411D9B966EE&yid=2DD7160C83D0ACED&vid=B6DA1AC076E37400&iid=0B39A22176CE99FB&sid=D5C9DC4EF2F78008&eid=ED01F5AE50BE09C0&journal_id=1674-7305&journal_name=ScienceChina.Lifesciences&referenced_num=0&reference_num=12