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Originally published In Press as doi:10.1074/jbc.M203713200 on May 21, 2002

J. Biol. Chem., Vol. 277, Issue 30, 27567-27574, July 26, 2002
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Differential Roles of JIP Scaffold Proteins in the Modulation of Amyloid Precursor Protein Metabolism*

Hidenori TaruDagger §, Yutaka KirinoDagger , and Toshiharu Suzuki§

From the Dagger  Laboratory of Neurobiophysics, School of Pharmaceutical Sciences, the University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033 and § Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku Kita-12, Nishi-6, Sapporo 060-0812, Japan

We previously found that the JNK-interacting proteins JIP1b and JIP2 associate with the cytoplasmic domain of the Alzheimer's amyloid precursor protein (APP) (Taru, H., Iijima, K., Hase, M., Kirino, Y., Yagi, Y., and Suzuki, T. (2002) J. Biol. Chem. 277, 20070-20078). This interaction involves the carboxyl-terminal phosphotyrosine interaction (PI) domain of JIP1b or JIP2 and the GYENPTY motif in the APP cytoplasmic domain. The expression of JIP1b stabilizes immature APP and suppresses the production of a secreted large extracellular amino-terminal domain of APP, the generation of a cleaved intracellular carboxyl-terminal fragment of APP, and the secretion of beta -amyloid 40 and 42. Deletion of the PI domain or alteration of PI amino acid residues prevents JIP1b from interacting with APP and affecting its metabolism, but deletion of the JNK-binding domain of JIP1b has no effect. JIP2, a weaker APP-binding protein, does not influence the processing of APP, although it is known that both JIP1b and JIP2 equally regulate the JNK signaling cascade. The present results suggest that JIP1b can directly modulate APP metabolism by interacting with the APP cytoplasmic domain, independent of its regulation of the JNK signaling cascade.

* This work was supported by grants-in-aid for Scientific Research on Priority Areas (C)-Advanced Brain Science Project TS 13210031 and 14017001, grants-in-aid for Scientific Research TS 12470494 and TS 11557179 from the Ministry of Education, Science, Culture, Sports, and Science and Technology, Japan, and the UEHARA Memorial Foundation (to T. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku Kita-12, Nishi-6, Sapporo 060-0812, Japan. Tel.: 81-11-706-3250; Fax: 81-11-706-4991; E-mail: tsuzuki@pharm.hokudai.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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