The insect homologue of the amyloid precursor protein interacts with the heterotrimeric G protein Goα in an identified population of migratory neurons

T. L. Swanson, L. M. Knittel, T. M. Coate, S. M. Farley, M. A. Snyder, P. F. Copenhaver

Research output: Contribution to journalArticle

25 Scopus citations


The amyloid precursor protein (APP) is the source of Aβ fragments implicated in the formation of senile plaques in Alzheimer's disease (AD). APP-related proteins are also expressed at high levels in the embryonic nervous system and may serve a variety of developmental functions, including the regulation of neuronal migration. To investigate this issue, we have cloned an orthologue of APP (msAPPL) from the moth, Manduca sexta, a preparation that permits in vivo manipulations of an identified set of migratory neurons (EP cells) within the developing enteric nervous system. Previously, we found that EP cell migration is regulated by the heterotrimeric G protein Goα: when activated by unknown receptors, Goα induces the onset of Ca2+ spiking in these neurons, which in turn down-regulates neuronal motility. We have now shown that msAPPL is first expressed by the EP cells shortly before the onset of migration and that this protein undergoes a sequence of trafficking, processing, and glycosylation events that correspond to discrete phases of neuronal migration and differentiation. We also show that msAPPL interacts with Goα in the EP cells, suggesting that msAPPL may serve as a novel G-protein-coupled receptor capable of modulating specific aspects of migration via Goα-dependent signal transduction.

Original languageEnglish (US)
Pages (from-to)160-178
Number of pages19
JournalDevelopmental Biology
Issue number1
StatePublished - Dec 1 2005



  • APP
  • Amyloid
  • G protein
  • Manduca sexta
  • Neuronal migration

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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