Recombinant Drosophila melanogaster Beta-amyloid-like protein (Appl), partial

1. Results show that Drosophila APPL-RNAi largely mimics transgenic amyloid beta in various phenotypes which include eye degeneration, reduced longevity and motor neuron deficit functions. This is the first report showing comparable phenotypes between APPL and amyloid beta in Alzheimer's disease model of Drosophila. PMID: 28336338
2. Appl siRNA inhibition in cortex glia resulted in longer sleep and reduced expression of genes involved in glutamate recycling. PMID: 28314820
3. memory is altered by two connected mechanisms-APPL loss-of-function and amyloid peptide toxicity-revealing in Drosophila a functional interaction between APPL and amyloid peptide. PMID: 26274614
4. The results of this study showed that increased production of the endogenous Drosophila Amyloid Intracellular Domain (dAICD) caused disruption of circadian rest-activity rhythms during aging. PMID: 25766673
5. Our data demonstrate that, in addition to secreted APPL, the noncleaved form is involved in memory, raising the possibility that secreted and full-length APPL act together in memory processes. PMID: 25609621
6. findings suggest that a normal function of presenilin (PS)is to repress kinesin-1 and dynein motor activity during axonal transport of amyloid precursor protein (APP) vesicles; perturbations of APP/PS transport could contribute to early neuropathology observed in Alzheimer's Disease PMID: 23710041
7. APPL is the first example of a modulator of the Wnt-PCP pathway specifically required for axon outgrowth. PMID: 23690751
8. Data show that Appl is directly regulated by the Ras/MAPK pathway through a mechanism mediated by PntP2. PMID: 23178937
9. [review] APP-like proteins are involved in neuronal differentiation, neuritic outgrowth, and synapse formation. PMID: 21912928
10. Disruption of amyloid protein precursor (APP) proteins and specifically their soluble alpha-cleaved ectodomains can protect against progressive neurodegeneration in vivo. PMID: 22266106
11. Down-regulation of the ATP-binding cassette transporter 2 (Abca2) reduces amyloid-beta production by altering Nicastrin maturation and intracellular localization. PMID: 22086926
12. accumulation of Ass42 plaques induces JNK signaling in neurons and induction of JNK contributes to Ass42 mediated cell death PMID: 21949710
13. Findings show that age-related changes in amyloid characteristics may be a trigger for late-onset polyglutamine diseases. PMID: 21466635
14. in adult flies, APPL is not required for learning but is specifically involved in long-term memory, a long lasting memory whose formation requires de novo protein synthesis and is thought to require synaptic structural plasticity. PMID: 21248128
15. Abeta42 levels were reduced upon GSK-3 inhibition, pointing to a direct role of GSK-3 in the regulation of Abeta42 peptide level, in the absence of APP processing. PMID: 20824130
16. Data suggest that toxic effects of amyloid beta-peptide aggregation in vivo can therefore be eliminated by sequestration of hydrophobic regions in monomeric peptides, even when these are extremely aggregation prone. PMID: 20305716
17. APP-Like (APPL) can induce postdevelopmental axonal arborization, which depends critically on a conserved motif in the C-terminus and requires interaction with the Abelson (Abl) tyrosine kinase. PMID: 16052209
18. Study shows that APP-BP1 specifically binds the intracellular domain of APP-like protein (APPL), APP-BP1 mutation partially suppresses the abnormal macrochaete phenotype of Appl(d), while overexpression of dAPP-BP1 causes abnormal macrochaetes. PMID: 16628230
19. These data offer insight into the toxicity of Abeta and open new areas for further study into Alzheimer's disease pathogenesis. PMID: 18245849
20. findings show that Abeta fragments aggregate into intracellular fibrils, amyloid deposits, and cause age-dependent behavioral deficits and neurodegeneration PMID: 19049874
21. yata mutants showed impaired subcellular localization of APPL. PMID: 19209226
22. Results demonstrate that 53 of the modifiers genetically interacted with APP, and characterization of these genes may provide valuable insights into Presenilin function in development and disease. PMID: 19241393

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KEGG: dme:Dmel_CG7727

STRING: 7227.FBpp0298292

UniGene: Dm.4862