Structural basis of interaction between protein tyrosine phosphatase PCP-2 and β-catenin |
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| Authors: | He Yaqin YAN Hexin DONG Hui ZHANG Peng TANG Liang QIU Xiuhua WU Mengchao WANG Hongyang |
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| Institution: | International Co-operation Laboratory on Signal Transduction, Eastern Hepatobiliary Surgery Hospital, Second Military Medical University, Shanghai 200438, China |
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| Abstract: | 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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| Keywords: | PCP-2 β-catenin protein tyrosine phosphatase interaction |
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