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Involvement of beta3A subunit of adaptor protein-3 in intracellular trafficking of receptor-like protein tyrosine phosphatase PCP-2.

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1
International Co-operation Laboratory on Signal Transduction, Eastern Hepatobiliary Surgery Institute, Second Military Medical University, Shanghai 200438, China.

Abstract

PCP-2 is a human receptor-like protein tyrosine phosphatase and a member of the MAM domain family cloned in human pancreatic adenocarcinoma cells. Previous studies showed that PCP-2 directly interacted with beta-catenin through the juxtamembrane domain, dephosphorylated beta-catenin and played an important role in the regulation of cell adhesion. Recent study showed that PCP-2 was also involved in the repression of beta-catenin-induced transcriptional activity. Here we describe the interactions of PCP-2 with the beta3A subunit of adaptor protein (AP)-3 and sorting nexin (SNX) 3. These protein complexes were detected using the yeast two-hybrid assay with the juxtamembrane and membrane-proximal catalytic domain of PCP-2 as "bait" Both AP-3 and SNX3 are molecules involved in intracellular trafficking of membrane receptors. The association between the beta3A subunit of AP-3 and PCP-2 was further confirmed in mammalian cells. Our results suggested a possible mechanism of intracellular trafficking of PCP-2 mediated by AP-3 and SNX3 which might participate in the regulation of PCP-2 functions.

PMID:
17622474
[Indexed for MEDLINE]
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