Neuronal development and homeostasis depend on effective cellular signalling and tight regulation of the molecules involved. Neurotrophins (NTs) are essential for the activation of neuronal receptors, such as catalytic tropomyosin receptor kinase (Trk) receptors and p75 nerve growth factor receptor (p75NTR). NTs and their activated receptors (NTRs) are constantly endocytosed and recycled, which is enabled by molecular motors, such as dynein. The dynein adaptor bicaudal-D1 (BICD1) has been described to be involved in endocytic sorting, but its molecular partners and the underlying mechanism are still unclear. In this study, Giampietro Schiavo and colleagues (Budzinska et al., 2020) show that the protein tyrosine phosphatase non-receptor type 23 (PTPN23), a member of the endosomal sorting complexes required for transport (ESCRT) machinery, interacts with BICD1 to regulate the sorting of activated NTRs in neurons. PTPN23 colocalises with BICD1 in these cells, but interacts with the N-terminus of BICD1 and not its cargo-binding domain. Furthermore, the authors observe that PTPN23, like BICD1, associates with TrkB-carrying endosomes. Accordingly, downregulation of PTPN23 leads to the accumulation of TrkB and p75NTR in enlarged compartments that contain early endosome markers, suggesting that lack of PTPN23 affects endosome maturation and thus proper sorting and distribution of NTRs. Taken together, this study uncovers a new role for PTPN23 in maintaining the endocytic flow in neurons.