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- W2014633008 abstract "Modifier of cell adhesion protein (MOCA; previously called presenilin [PS] binding protein) is a DOCK180-related molecule, which interacts with PS1 and PS2, is localized to brain areas involved in Alzheimer's disease (AD) pathology, and is lost from the soluble fraction of sporadic Alzheimer's disease (AD) brains. Because PS1 has been associated with gamma-secretase activity, MOCA may be involved in the regulation of beta-amyloid precursor protein (APP) processing. Here we show that the expression of MOCA decreases both APP and amyloid beta-peptide secretion and lowers the rate of cell-substratum adhesion. In contrast, MOCA does not lower the secretion of amyloid precursor-like protein (APLP) or several additional type 1 membrane proteins. The phenotypic changes caused by MOCA are due to an acceleration in the rate of intracellular APP degradation. The effect of MOCA expression on the secretion of APP and cellular adhesion is reversed by proteasome inhibitors, suggesting that MOCA directs nascent APP to proteasomes for destruction. It is concluded that MOCA plays a major role in APP metabolism and that the effect of MOCA on APP secretion and cell adhesion is a downstream consequence of MOCA-directed APP catabolism. This is a new mechanism by which the expression of APP is regulated." @default.
- W2014633008 created "2016-06-24" @default.
- W2014633008 creator A5014708668 @default.
- W2014633008 creator A5072742742 @default.
- W2014633008 creator A5076764999 @default.
- W2014633008 date "2002-07-01" @default.
- W2014633008 modified "2023-09-25" @default.
- W2014633008 title "A novel mechanism for the regulation of amyloid precursor protein metabolism" @default.
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- W2014633008 doi "https://doi.org/10.1083/jcb.200110151" @default.
- W2014633008 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2173011" @default.
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