Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease

European Journal of Neuroscience

Volumn 11, Issue 6, 1999, Pages 1988-1994

  McLoughlin, Declan M ^a   Irving, Nicholas G ^a   Brownlees, Janet ^a   Brion, Jean Pierre ^b   Leroy, Karelle ^b   Miller, Christopher C J ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

Author keywords

APP; Fe65; Human; Rodent

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BRAIN PROTEIN; PHOSPHOTYROSINE;

ALZHEIMER DISEASE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BRAIN CELL; CARBOXY TERMINAL SEQUENCE; CHO CELL; CONTROLLED STUDY; HUMAN; HUMAN TISSUE; MOLECULAR CLONING; MOUSE; NEUROFIBRILLARY TANGLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN METABOLISM; SENILE PLAQUE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN PRECURSOR; ANIMALS; BRAIN; CADHERINS; CARRIER PROTEINS; CHO CELLS; CRICETINAE; HOMEOSTASIS; HUMANS; MICE; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; SENILE PLAQUES; SUBCELLULAR FRACTIONS; TISSUE DISTRIBUTION; TRANSFECTION;

EID: 0033006807     PISSN: 0953816X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1460-9568.1999.00610.x     Document Type: Article

References (7)

1. Blanco, G., Irving, N.G., Brown, S.D.M., Miller, C.C.J. & McLoughlin, D.M. (1998) Mapping of the human and murine X11-like genes (APBA2 and Apba2), the murine Fe65 gene (Apbbl) and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein. Mamm. Genome, 9, 473-479.
2. Borg, J.-P., Ooi, J. Levy, E. & Margolis, B. (1996) The phosphotyrosine interaction domains of X11 and Fe65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol., 16, 6229-6241.
3. Borg, J.P., Yang, Y.N., De Taddéo-Borg, M., Margolis, B. & Turner, R.S. (1998) The X11α protein slows cellular amyloid precursor protein processing and reduces Aβ40 and A(β42 secretion. J. Biol. Chem., 273, 14761-14766.
4. Bredt, D.S. (1998) Sorting out genes that regulate epithelial and neuronal polarity. Cell, 94, 691-694.
5. Breen, K., Bruce, M. & Anderton, B.H. (1991) β-amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion. J. Neurosci. Res., 28, 90-100.
6. Bressler, S.L., Gray, M.D., Sopher, B.L., Hu, Q.B., Hearn, M.G., Pham, D.G., Dinulos, M.B., Fukuchi, K.I., Sisodia, S.S., Miller, M.A., Disteche, C.M. & Martin, G.M. (1996) cDNA cloning and chromosome mapping of the human Fe65 gene: Interaction of the conserved cytoplasmic domains of the human β-amyloid precursor protein and its homologues with the mouse Fe65 protein. Hum. Mol. Genet., 5, 1589-1598.
7. Butz, S., Okamoto, M. & Sudhof, T.C. (1998) A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in the brain. Cell, 94, 773-782.