The BioGRID | PUBLICATION VIEW

	J. Biol. Chem. Jul (2000); 275(30):23134-8
Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein.
Lee DS, Tomita S, Kirino Y, Suzuki T
Laboratory of Neurobiophysics, School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan.
Abstract: We isolated a cDNA encoding a novel protein, XB51, that interacts with the amino-terminal domain of the neuron-specific X11-like protein (X11L). The protein XB51 inhibited the association of X11L with amyloid precursor protein through a non-competitive mechanism and abolished the suppression of beta-amyloid production by X11L. The majority of XB51 is localized around the nucleus and recovered in 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS) buffer-insoluble fraction when XB51 is expressed in cells. Association of XB51 with X11L changed the intracellular distribution of XB51 and resulted in redistribution of XB51 into the CHAPS buffer-soluble fraction. These observations suggest that XB51, together with X11L, plays an important role in the regulatory system of amyloid precursor protein metabolism and beta-amyloid generation.
[PUBMED: 10833507]