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The Journal of Neuroscience, September 1, 2001, 21(17):6597-6607

c-Jun N-Terminal Kinase (JNK)-Interacting Protein-1b/Islet-Brain-1 Scaffolds Alzheimer's Amyloid Precursor Protein with JNK

Shuji Matsuda¹, Takashi Yasukawa¹, Yasuko Homma¹, Yuko Ito¹, Takako Niikura¹, Takako Hiraki¹, Shuichi Hirai², Shigeo Ohno², Yoshiko Kita¹, Masaoki Kawasumi¹, Keisuke Kouyama¹, Tokuo Yamamoto³, John M. Kyriakis⁴, and Ikuo Nishimoto¹

¹ Department of Pharmacology and Neurosciences, KEIO University School of Medicine, Shinjuku-ku, Tokyo 160-8582, Japan, ² Department of Molecular Biology, Yokohama City University School of Medicine, Kanazawa-ku, Yokohama 236-0004, Japan, ³ Tohoku University Gene Research Center, Aoba-ku, Sendai 981-8555, Japan, and ⁴ Diabetes Research Laboratory, Massachusetts General Hospital-East, Charlestown, Massachusetts 02129

Using a yeast two-hybrid method, we searched for amyloid precursor protein (APP)-interacting molecules by screening mouse and human brain libraries. In addition to known interacting proteins containing a phosphotyrosine-interaction-domain (PID)Fe65, Fe65L, Fe65L2, X11, and mDab1, we identified, as a novel APP-interacting molecule, a PID-containing isoform of mouse JNK-interacting protein-1 (JIP-1b) and its human homolog IB1, the established scaffold proteins for JNK. The APP amino acids Tyr⁶⁸², Asn⁶⁸⁴, and Tyr⁶⁸⁷ in the G⁶⁸¹YENPTY⁶⁸⁷ region were all essential for APP/JIP-1b interaction, but neither Tyr⁶⁵³ nor Thr⁶⁶⁸ was necessary. APP-interacting ability was specific for this additional isoform containing PID and was shared by both human and mouse homologs. JIP-1b expressed by mammalian cells was efficiently precipitated by the cytoplasmic domain of APP in the extreme Gly⁶⁸¹-Asn⁶⁹⁵ domain-dependent manner. Reciprocally, both full-length wild-type and familial Alzheimer's disease mutant APPs were precipitated by PID-containing JIP constructs. Antibodies raised against the N and C termini of JIP-1b coprecipitated JIP-1b and wild-type or mutant APP in non-neuronal and neuronal cells. Moreover, human JNK11 formed a complex with APP in a JIP-1b-dependent manner. Confocal microscopic examination demonstrated that APP and JIP-1b share similar subcellular localization in transfected cells. These data indicate that JIP-1b/IB1 scaffolds APP with JNK, providing a novel insight into the role of the JNK scaffold protein as an interface of APP with intracellular functional molecules.

Key words: JIP-1b/IB1; amyloid precursor protein; phosphotyrosine-interaction-domain; scaffolding protein; c-Jun N-terminal kinase

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Copyright © 2001 Society for Neuroscience  0270-6474/01/21176597-11$05.00/0

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