Secretory carrier-associated membrane protein 2 (SCAMP2)

Secretory carrier-associated membrane protein 2 (SCAMP2) is an integral membrane protein belonging to the SCAMP family, which is highly conserved across the animal and plant kingdoms[2][3][4][5][7]. SCAMP2 contains four transmembrane domains and is most notably involved in the regulation of membrane trafficking, with prominent roles in post-Golgi recycling pathways and granule exocytosis, especially in neuroendocrine and secretory cells[1][3][5][7]. SCAMP2 is concentrated at intracellular vesicles as well as at the plasma membrane—specifically at exocytotic docking/fusion sites, where it collaborates with SNARE proteins to facilitate the final steps of vesicle fusion and secretion[1]. Its central "E peptide" domain is essential for its function in exocytosis; mutations here disrupt regulated secretion[1]. Additionally, SCAMP2 (and SCAMP5) have been reported as potential diagnostic and prognostic biomarkers for acute myeloid leukemia, but SCAMP2 is not currently classified as a therapeutic target, and there are no approved drugs that act on this protein[6].

Other names

secretory carrier membrane protein 2secretory carrier-associated membrane protein 2SCAMP2testis secretory sperm-binding protein Li 219p

Not applicable; no drugs targeting this molecule are described