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Journal of Biochemistry 2006 139(5):931-939; doi:10.1093/jb/mvj105
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© 2006 The Japanese Biochemical Society.

Regular Paper

CIN85 Is Localized at Synapses and Forms a Complex with S-SCAM via Dendrin

Akira Kawata, Junko Iida, Mitsunobu Ikeda, Yuji Sato, Hiroki Mori, Ai Kansaku, Kazutaka Sumita, Naoyuki Fujiwara, Chiaki Rokukawa, Mamiko Hamano, Susumu Hirabayashi and Yutaka Hata*

Department of Medical Biochemistry, Graduate School of Medicine, Tokyo Medical and Dental University, Tokyo 113-8519

* To whom correspondence should be addressed. Tel: +81-3-5803-5164, Fax: +81-3-5803-0121, E-mail: yuhammch{at}med.tmd.ac.jp

Membrane-associated guanylate kinase inverted (MAGI)-1 plays a role as a scaffold at cell junctions in non-neuronal cells, while S-SCAM, its neuronal isoform, is involved in the organization of synapses. A search for MAGI-1–interacting proteins by yeast two-hybrid screening of a kidney cDNA library yielded dendrin. As dendrin was originally reported as a brain-specific postsynaptic protein, we tested the interaction between dendrin and S-SCAM and revealed that dendrin binds to the WW domains of S-SCAM. Dendrin is known to be dendritically translated but its function is largely unknown. To gain insights into the physiological meaning of the interaction, we performed a second yeast two-hybrid screening using dendrin as a bait. We identified CIN85, an endocytic scaffold protein, as a putative dendrin-interactor. Immunocytochemistry and subcellular fractionation analysis supported the synaptic localization of CIN85. The first SH3 domain and the C-terminal region of CIN85 bind to the proline-rich region and the N-terminal region of dendrin, respectively. In vitro experiments suggest that dendrin forms a ternary complex with CIN85 and S-SCAM and that this complex formation facilitates the recruitment of dendrin and S-SCAM to vesicle-like structures where CIN85 is accumulated.


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