PCP-2 is a member of receptor-like protein tyrosine phosphatase of the MAM do-main family.To investigate which part of PCP-2 was involved in its interaction withβ-catenin,we constructed various deletion mutants of PC...PCP-2 is a member of receptor-like protein tyrosine phosphatase of the MAM do-main family.To investigate which part of PCP-2 was involved in its interaction withβ-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 withβ-catenin individually.An in vivo binding assay revealed that the expression of wild-type PCP-2,PCP-2?C1C2(deleted PCP-2 without both PTP domains)and PCP-2?C2(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 andβ-catenin could associate directly and the juxtamembrane region in PCP-2 was sufficient for the process.展开更多
基金This work was supported by the National Natural Science Foundation of China(Grant Nos.30270686 and 30370740)the Key Research Project(30110811 and 03DJ14007).
文摘PCP-2 is a member of receptor-like protein tyrosine phosphatase of the MAM do-main family.To investigate which part of PCP-2 was involved in its interaction withβ-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 withβ-catenin individually.An in vivo binding assay revealed that the expression of wild-type PCP-2,PCP-2?C1C2(deleted PCP-2 without both PTP domains)and PCP-2?C2(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 andβ-catenin could associate directly and the juxtamembrane region in PCP-2 was sufficient for the process.
