SCAMP2 (secretory carrier membrane protein 2) is a key regulator of membrane protein trafficking and exocytosis, functioning primarily in post-Golgi recycling pathways. The protein acts as a trafficking regulator by controlling the cell surface targeting of various membrane proteins through its interaction with recycling endosomes 12. SCAMP2 modulates the surface expression of critical transporters including the renal Na-K-2Cl co-transporter NKCC2, where it decreases exocytotic trafficking and limits plasma membrane insertion 1. Similarly, SCAMP2 interacts with the serotonin transporter (SERT) and reduces its cell surface abundance, thereby decreasing serotonin uptake activity 2. The protein's regulatory function depends on a conserved cytoplasmic E peptide, particularly cysteine-201, which is essential for its trafficking control mechanisms 12. SCAMP2 also facilitates exocytotic fusion pore formation by linking Arf6 and phospholipase D1 function in neuroendocrine cells 3. Additionally, SCAMP2 positively regulates vitamin C transport by enhancing hSVCT1 function, impacting both epithelial absorption and neuronal differentiation 4. In disease contexts, SCAMP2 expression is elevated in acute myeloid leukemia and serves as a potential diagnostic marker 5, while also being associated with post-COVID-19 neurological changes 6.