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J Biol Chem, Vol. 273, Issue 24, 14761-14766, June 12, 1998
Protein Slows Cellular Amyloid Precursor Protein
Processing and Reduces A
40 and A42 Secretion
,,¶, and
From the Constitutive amyloid precursor protein (APP)
metabolism results in the generation of soluble APP (APPs) and A Howard Hughes Medical Institute,
¶ Department of Internal Medicine and Biological Chemistry, and
§ Department of Neurology, University of Michigan Medical
Center, Ann Arbor, Michigan 48109 and Veterans Affairs Medical
Center Geriatric Research, Education, and Clinical Center,
Ann Arbor, Michigan 48105
peptides, including A40 and A42-the major component of amyloid
plaques in Alzheimer's disease brain. The phosphotyrosine binding
(PTB) domain of X11 binds to a peptide containing a YENPTY motif found
in the carboxyl terminus of APP. We have cloned the full-length
X11 gene now referred to as X11
.
Coexpression of X11 with APP results in comparatively greater levels
of cellular APP and less APPs, A40, and A42 recovered in
conditioned medium of transiently transfected HEK 293 cells. These
effects are impaired by a single missense mutation of either APP (Y682G
within the YENPTY motif) or X11 (F608V within the PTB domain), which
diminishes their interaction, thus demonstrating specificity. The
inhibitory effect of X11 on A40 and A42 secretion is amplified
by coexpression with the Swedish mutation of APP (K595N/M596L), which
promotes its amyloidogenic processing. Pulse-chase analysis
demonstrates that X11 prolongs the half-life of APP from ~2 h to
~4 h. The effects of X11 on cellular APP and APPs recovery were
confirmed in a 293 cell line stably transfected with APP. The specific
binding of the PTB domain of X11 to the YENPTY motif-containing
peptide of APP appears to slow cellular APP processing and thus reduces
recovery of its soluble fragments APPs, A40, and A42 in
conditioned medium of transfected HEK 293 cells. X11 may be involved
in APP trafficking and metabolism in neurons and thus may be implicated
in amyloidogenesis in normal aging and Alzheimer's disease brain.
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J.-P. Borg, M. O. Lopez-Figueroa, M. de Taddeo-Borg, D. E. Kroon, R. S. Turner, S. J. Watson, and B. Margolis Molecular Analysis of the X11-mLin-2/CASK Complex in Brain J. Neurosci., February 15, 1999; 19(4): 1307 - 1316. [Abstract] [Full Text] [PDF]
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S. Tomita, T. Ozaki, H. Taru, S. Oguchi, S. Takeda, Y. Yagi, S. Sakiyama, Y. Kirino, and T. Suzuki Interaction of a Neuron-specific Protein Containing PDZ Domains with Alzheimer's Amyloid Precursor Protein J. Biol. Chem., January 22, 1999; 274(4): 2243 - 2254. [Abstract] [Full Text] [PDF]
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J.-P. Borg, S. W. Straight, S. M. Kaech, M. de Taddeo-Borg, D. E. Kroon, D. Karnak, R. S. Turner, S. K. Kim, and B. Margolis Identification of an Evolutionarily Conserved Heterotrimeric Protein Complex Involved in Protein Targeting J. Biol. Chem., November 27, 1998; 273(48): 31633 - 31636. [Abstract] [Full Text] [PDF]
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S. Tomita, T. Fujita, Y. Kirino, and T. Suzuki PDZ Domain-dependent Suppression of NF-kappa B/p65-induced Abeta 42 Production by a Neuron-specific X11-like Protein J. Biol. Chem., April 21, 2000; 275(17): 13056 - 13060. [Abstract] [Full Text] [PDF]
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G. Minopoli, P. de Candia, A. Bonetti, R. Faraonio, N. Zambrano, and T. Russo The beta -Amyloid Precursor Protein Functions as a Cytosolic Anchoring Site That Prevents Fe65 Nuclear Translocation J. Biol. Chem., February 23, 2001; 276(9): 6545 - 6550. [Abstract] [Full Text] [PDF]
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H. Misawa, Y. Kawasaki, J. Mellor, N. Sweeney, K. Jo, R. A. Nicoll, and D. S. Bredt Contrasting Localizations of MALS/LIN-7 PDZ Proteins in Brain and Molecular Compensation in Knockout Mice J. Biol. Chem., March 16, 2001; 276(12): 9264 - 9272. [Abstract] [Full Text] [PDF]
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