Nerve growth factor (NGF) can bind to cell surface receptor p75NTR and TrkA and play a vital role in cell differentiation, survival, apoptosis, proliferation and migration. TrkA interacted with multiple proteins in vivo, but due to the complexity of the NGF signaling pathway, it is still necessary to explore more proteins that interact with TrkA to gain a more accurate understanding of the NGF pathway. Here we report eIF4A1 is a new partner of TrkA. We found eIF4A1 interacted with TrkA via the yeast two hybrid assay. And then the association between TrkA and eIF4A1 was identified by GST pull-down and co-immunoprecipitation assay. Additionally, NGF stimulated this interaction and the associated binding domain is the N-terminus domain (NTD) in eIF4A1 and the TK domain in TrkA. And eIF4A1 could colocalize with TrkA at cell membrane. Furthermore, eIF4A1 also inhibits TrkA polyubiquitination through lysine (Lys)-63-linked polyubiquitin chains which causes its internalization. So eIF4A1 plays a novel role in NGF signaling pathway.