Watanabe-Kaneko Keiko, Sonoda Tomoko, Miyagi Yohei, Yamashita Tetsuji, Okuda Kenji, Kawamoto Susumu
Department of Molecular Biodefense Research, Yokohama City University Graduate School of Medicine, Yokohama, Japan.
Neuroreport. 2007 Mar 26;18(5):489-93. doi: 10.1097/WNR.0b013e3280586821.
Delphilin, which interacts with a glutamate receptor (GluR) delta2-subunit, is a postsynaptic density scaffolding protein at the cerebellar parallel fiber-Purkinje cell synapses. Delphilin specifically interacts with the GluRdelta2 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 GluRdelta2. 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 GluRdelta2-Delphilin-monocarboxylate transporter 2 complex in synaptic membranes.
德尔菲林与谷氨酸受体（GluR）δ2亚基相互作用，是小脑平行纤维-浦肯野细胞突触处的一种突触后致密支架蛋白。德尔菲林通过其突触后致密蛋白95/盘状大蛋白/ZO-1（PDZ）结构域与GluRδ2的C末端特异性相互作用。由于许多含PDZ的支架蛋白可与多种膜蛋白结合，我们推测德尔菲林可能除了GluRδ2之外还有其他结合伴侣。为了寻找德尔菲林与其他结合蛋白之间的联系，我们通过表面等离子体共振分析在浦肯野细胞中定位的候选膜蛋白中进行筛选。结果，我们发现单羧酸转运蛋白2的C末端与德尔菲林PDZ特异性且显著结合，并且在突触膜中可能存在GluRδ2-德尔菲林-单羧酸转运蛋白2复合物。
