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 beta-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 beta-catenin individually. An in vivo binding assay revealed that the expression of wild-type PCP-2, PCP-2 deltaC1C2 (deleted PCP-2 without both PTP domains) and PCP-2 deltaC2 (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 beta-catenin could associate directly and the juxtamembrane region in PCP-2 was sufficient for the process.
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