SLC18B1 encodes the vesicular polyamine transporter (VPAT), which loads polyamines into secretory vesicles to enable their regulated exocytosis across multiple cell types (PMID:25355561, PMID:31800589). Purified human SLC18B1 reconstituted into proteoliposomes actively transports spermine and spermidine by H+ antiport, driven by an electrochemical H+ gradient, and the protein localizes to vesicles in astrocytes where its knockdown lowers cellular polyamine content (PMID:25355561). VPAT also handles monoamines and depends on the V-ATPase-generated H+ gradient; in mast cells it operates upstream of histamine release, with its knockdown abolishing polyamine exocytosis (PMID:32004521). Vesicular, Ca2+-dependent polyamine secretion via VPAT is similarly demonstrated in megakaryoblastic MEG-01 cells and platelets, where release is sensitive to bafilomycin A1 (V-ATPase inhibition), reserpine, and VPAT inhibitors (PMID:38527572). In vivo, Slc18b1 knockout mice show reduced brain polyamine content, impaired short- and long-term memory, altered expression of LTP/calcium-signalling/synaptic genes, and partial diazepam resistance, establishing VPAT as required for normal brain polyamine homeostasis and GABAergic/glutamatergic signalling (PMID:31800589).