![]() Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Binding to DAB1 inhibits its serine phosphorylation. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, JIP1, SHC1 and, NUMB and DAB1. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Induces a RAGE-dependent pathway that activates p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Involved in copper homeostasis/oxidative stress through copper ion reduction. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Can promote transcription activation through binding to Fe65-Tip60 and inhibits Notch signaling through interaction with Numb. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis. The Abeta peptide is released from the cell, its extracellular deposition and accumulation form the main components of amyloid plaques in Alzheimer's disease. ![]() Cleaved by secretases to form a number of peptides, some of which bind to the acetyltransferase complex Fe65/TIP60 to promote transcriptional activation. APP: a cell surface receptor that influences neurite growth, neuronal adhesion and axonogenesis. ![]()
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