ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013
Amyloid precursor proteins interact with the heterotrimeric G protein Go in the control of neuronal migration.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- IDRdecoder: a machine learning approach for rational drug discovery toward intrinsically disordered regions.Frontiers in bioinformatics · 2025Article
- Article
- Fasciclin 2 plays multiple roles in promoting cell migration within the developing nervous system of Manduca sexta.Developmental biology · 2023Article
- Single-synapse analyses of Alzheimer's disease implicate pathologic tau, DJ1, CD47, and ApoE.Science advances · 2021Article
- Impact of a discordant helix on β-amyloid structure, aggregation ability and toxicity.European biophysics journal : EBJ · 2017Review
- Embryonic mosaic deletion of APP results in displaced Reelin-expressing cells in the cerebral cortex.Developmental biology · 2017Article
- Role of APP Interactions with Heterotrimeric G Proteins: Physiological Functions and Pathological Consequences.Frontiers in molecular neuroscience · 2017Review
- Amyloid Precursor Protein family as unconventional Go-coupled receptors and the control of neuronal motility.Neurogenesis (Austin, Tex.) · 2017Review
- Neuronal migration during development and the amyloid precursor protein.Current opinion in insect science · 2016Review
- Manduca Contactin Regulates Amyloid Precursor Protein-Dependent Neuronal Migration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- APP Receptor? To Be or Not To Be.Trends in pharmacological sciences · 2016Review
- Analysis of Amyloid Precursor Protein Function in Drosophila melanogaster.Frontiers in molecular neuroscience · 2016Review
- Amyloid Precursor Proteins Are Dynamically Trafficked and Processed during Neuronal Development.Frontiers in molecular neuroscience · 2016Article
- Visualizing K48 Ubiquitination during Presynaptic Formation By Ubiquitination-Induced Fluorescence Complementation (UiFC).Frontiers in molecular neuroscience · 2016Article
- Role ofFrontiers in molecular neuroscience · 2016Review
- The APP Intracellular Domain Is Required for Normal Synaptic Morphology, Synaptic Plasticity, and Hippocampus-Dependent Behavior.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Synaptotagmins interact with APP and promote Aβ generation.Molecular neurodegeneration · 2015Article
- Dynamic self-guiding analysis of Alzheimer's disease.Oncotarget · 2015Review
- PAT1 inversely regulates the surface Amyloid Precursor Protein level in mouse primary neurons.BMC neuroscience · 2015Article
- The spinal muscular atrophy with pontocerebellar hypoplasia gene VRK1 regulates neuronal migration through an amyloid-β precursor protein-dependent mechanism.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Amyloid precursor protein (APP) belongs to a family of evolutionarily conserved transmembrane glycoproteins that has been proposed to regulate multiple aspects of cell motility in the nervous system. Although APP is best known as the source of β-amyloid fragments (Aβ) that accumulate in Alzheimer's disease, perturbations affecting normal APP signaling events may also contribute to disease progression. Previous in vitro studies showed that interactions between APP and the heterotrimeric G protein Goα-regulated Goα activity and Go-dependent apoptotic responses, independent of Aβ. However, evidence for authentic APP-Go interactions within the healthy nervous system has been lacking. To address this issue, we have used a combination of in vitro and in vivo strategies to show that endogenously expressed APP family proteins colocalize with Goα in both insect and mammalian nervous systems, including human brain. Using biochemical, pharmacological, and Bimolecular Fluorescence Complementation assays, we have shown that insect APP (APPL) directly interacts with Goα in cell culture and at synaptic terminals within the insect brain, and that this interaction is regulated by Goα activity. We have also adapted a well characterized assay of neuronal migration in the hawkmoth Manduca to show that perturbations affecting APPL and Goα signaling induce the same unique pattern of ectopic, inappropriate growth and migration, analogous to defective migration patterns seen in mice lacking all APP family proteins. These results support the model that APP and its orthologs regulate conserved aspects of neuronal migration and outgrowth in the nervous system by functioning as unconventional Goα-coupled receptors.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.