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J. Biol. Chem., Vol. 276, Issue 43, 40353-40361, October 26, 2001
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From the Neuronal Fe65 is an adapter protein that
interacts with the cytoplasmic domain of the
Phosphorylation-dependent Regulation of the
Interaction of Amyloid Precursor Protein with Fe65 Affects the
Production of
-Amyloid*
§,¶,
,, and¶**
Laboratory of Neurobiophysics, School of
Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033 Japan, the Department of Molecular
Biophysics and Biochemistry, Yale University School of Medicine, New
Haven, Connecticut 06510, and the ¶ Laboratory of Neuroscience,
Graduate School of Pharmaceutical Sciences, Hokkaido University,
Kita-12 Nishi -6, Kita-ku, Sapporo 060-0812, Japan
-amyloid precursor
protein (APP). Although the interaction has been reported to
occur between the second phosphotyrosine interaction domain of Fe65 and
the YENPTY motif in the cytoplasmic domain of APP, the regulatory
mechanism and biological function of this interaction remain unknown.
We report here that (i) a single amino acid mutation at the Thr-668
residue of APP695, located 14 amino acids toward the amino-terminal end from the 682YENPTY687 motif,
reduced the interaction between members of the Fe65 family of proteins
and APP, whereas interaction of APP with the phosphotyrosine interaction domain of other APP binders such as X11-like and mammalian disabled-1 was not influenced by this mutation; (ii) the
phosphorylation of APP at Thr-668 diminished the interaction of
APP with Fe65 by causing a conformational change in the cytoplasmic
domain that contains the Fe65-binding motif, YENPTY; and (iii) the
expression of Fe65 slightly suppressed maturation of APP and decreased
production of -amyloid (A). Mutation at Thr-668 of APP abolished
the effect of Fe65 on APP maturation. This mutation blocked the
Fe65-dependent suppression of A production and resulted
in the release of increased levels of A in the presence of Fe65. We
previously reported that during maturation of APP in neurons, the
protein is specifically phosphorylated at Thr-668 and undergoes
O-glycosylation. The present results suggest that
the phosphorylation of O-glycosylated mature APP at Thr-668
causes a conformational change in its cytoplasmic domain that prevents
binding of Fe65 in neurons and may lead to an alteration in the
production of A.
*
This work was supported by a grant-in-aid for Scientific
Research on Priority Areas C (Advanced Brain Science Project, TS 13210031) and B (TS 12470494) from the Ministry of Education, Science,
Culture, Sports, and Science and Technology (Japan).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.
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