MOLECULAR NEUROSCIENCEThe synaptic scaffolding protein Delphilin interacts with monocarboxylate transporter 2Watanabe-Kaneko, Keikoa; Sonoda, Tomokoa; Miyagi, Yoheib; Yamashita, Tetsujia; Okuda, Kenjia; Kawamoto, Susumua cAuthor Information aDepartment of Molecular Biodefense Research, Yokohama City University Graduate School of Medicine bMolecular Pathology and Genetics Division, Kanagawa Cancer Center Research Institute, Yokohama cDepartment of Molecular Function, Research Center for Pathogenic Fungi and Microbial Toxicoses, Chiba University, Chiba, Japan Correspondence to Dr Susumu Kawamoto, Research Center for Pathogenic Fungi and Microbial Toxicoses, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba 260-8673, Japan Tel: +81 43 226 2494; fax: +81 43 226 2486; e-mail: firstname.lastname@example.org Received 25 September 2006; accepted 5 December 2006 NeuroReport: March 26th, 2007 - Volume 18 - Issue 5 - p 489-493 doi: 10.1097/WNR.0b013e3280586821 Buy SDC Metrics Abstract Delphilin, which interacts with a glutamate receptor (GluR) δ2-subunit, is a postsynaptic density scaffolding protein at the cerebellar parallel fiber-Purkinje cell synapses. Delphilin specifically interacts with the GluRδ2 C-terminus via its postsynaptic density-95/discs-large/ZO-1 (PDZ) domain. As a number of PDZ-containing scaffolding proteins bind to several membrane proteins, we expected that Delphilin might also have other binding partners besides GluRδ2. To search for the link between Delphilin and other binding proteins, we carried out screening among candidate membrane proteins localized in Purkinje cells by surface plasmon resonance analyses. As a result, we found that the C-terminus of the monocarboxylate transporter 2 binds specifically and significantly with Delphilin PDZ and there is a probable existence of GluRδ2-Delphilin-monocarboxylate transporter 2 complex in synaptic membranes. © 2007 Lippincott Williams & Wilkins, Inc.