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Biochemical and Functional Interaction between VPAC1 and S‐SCAM/MAGI‐2

The vasoactive intestinal peptide (VIP) is 28 amino acid neuropeptide which has a wide distribution in peripheral and central nervous systems and a large spectrum of biological actions in mammals. VIP actions are mediated through specific G protein‐coupled receptors; VPAC1 and VPAC2. The synaptic scaffolding molecule S‐SCAM/MAGI2 is an adaptor protein which has six PDZ domains (PDZ0 to PDZ5), one GK domain, and two WW domains. Using yeast‐two‐hybrid assay, it was found that PDZ1 and PDZ2 domains of rat S‐SCAM/MAGI‐2 interact with the C‐terminus of mouse VIP receptor 1 (VPAC1). The S‐SCAM‐VPAC1 interaction was also verified by co‐immunoprecipitation in HEK293 cells with heterologous expressions. To examine the effect of S‐SCAM/MAGI‐2 on the surface expression of VPAC1, the surface biotinylation assay and surface immunocytochemistry were performed. Interestingly, VPAC1 expression on plasma membrane was increased by S‐SCAM/MAGI‐2. VPAC1 is coupled to Gs proteins and the activation of VPAC1 by ligand binding increases the intracellular concentration of cAMP. Accordingly, overexpression of S‐SCAM altered cellular responses evoked by VPAC1 stimulations through cAMP/PKA signals. These results suggest that S‐SCAM/MAGI‐2 binds to and regulates the activity of VPAC1.