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Aberrant metabolism of the amyloid precursor protein (APP) is believed to be at least part of the pathogenic process in Alzheimer's disease. The carboxy-terminus of APP has been shown to interact with the Mint/X11 family of phosphotyrosine binding (PTB) domain-bearing proteins. It is via their PTB domains that the Mints/X11s bind to APP. Here we report the cloning of full-length mouse Mint2 and demonstrate that in primary cortical neurons, Mint2 and APP share highly similar distributions. Mint2 also colocalizes with APP in transfected CHO cells. In Mint2/APP-cotransfected cells, Mint2 reorganizes the subcellular distribution of APP and also increases the steady-state levels of APP. Finally, we demonstrate that Mint2 is associated with the neuritic plaques found in Alzheimer's disease but not with neurofibrillary tangles. These results are consistent with a role for Mint2 in APP metabolism and trafficking, and suggest a possible role for the Mints/X11s in the pathogenesis of Alzheimer's disease.

Type

Journal article

Journal

Eur J Neurosci

Publication Date

06/1999

Volume

11

Pages

1988 - 1994

Keywords

Alzheimer Disease, Amino Acid Sequence, Amyloid beta-Protein Precursor, Animals, Brain, CHO Cells, Cadherins, Carrier Proteins, Cricetinae, Homeostasis, Humans, Mice, Molecular Sequence Data, Nerve Tissue Proteins, Plaque, Amyloid, Subcellular Fractions, Tissue Distribution, Transfection