Nerve growth factor (NGF) is one of the best-known examples of target-derived factors that regulate neuronal development. The biological processes of endocytosis and retrograde trafficking of NGF and its receptor, TrkA, are key mechanisms by which target-derived NGF influences neurons. We previously found the axon-derived TrkA elicits anterograde transport of naïve somatic TrkA via transcytosis. However, it is unclear whether the transcytosis machinery is a general mechanism which NGF utilizes to recruit additional membrane proteins necessary for axon growth and maturation. Here we report that amyloid-beta precursor protein (APP) is co-transcytosed with TrkA. Neurotrophin stimulation on distal axons induces co-localization and subsequent anterograde transport of somatic Trk receptors and APP. APP interacts with TrkA through its juxta-membrane domain, the domain that induces the formation of neurite-like processes in non-neuronal cells. The TrkA-APP interaction may also regulate proteolytic processing of APP. These data suggest that the TrkA-APP co-transcytosis is involved in NGF-dependent axon outgrowth and APP metabolism. Since APP and its proteolytic products play an important role in pathogenesis of Alzheimer’s disease (AD), our data further implicate that the deficit of TrkA-APP transcytosis is related to the onset of AD.