APP interacts with KCC2 to limit the latter from tyrosine-phosphorylation and ubiquitination and thus subsequent degradation, revealing a novel molecular pathway in which APP regulates GABAergic signaling and thus inhibition in the hippocampus.
A recent report proposing that the dpp stripe (the main source of the protein dpp) is dispensable for Drosophila wing disc growth missed the critical role on growth due to imprecise spatial removal of dpp.
APP mutations that either cause or prevent dementia alter APP metabolism in a complex and opposite fashion, suggesting a link between multiple APP processing events, dementia and ageing-dependent cognitive decline.
Amyloid precursor protein expression and accumulation of its intracellular fragment are required for exuberant neurite outgrowth associated with pathological presenilin 1 loss-of-function mutations before the emergence of amyloid burden in mice.
Oligomeric Amyloid-β and Tau, two proteins involved in Alzheimer's disease pathogenesis, require Amyloid Precursor Protein to enter neurons and exert their detrimental effect on synaptic plasticity and memory.
The survival of Drosophila amacrine neurons is controlled by neurotrophic signaling mediated by interactions between the cell surface protein DIP-γ and its partner Dpr11, which is expressed on presynaptic photoreceptors.
Reducing Akt-mediated huntingtin phosphorylation decreases APP accumulation at the synapse by reducing its anterograde axonal transport and ameliorates learning and memory in a mouse model of familial Alzheimer disease.