| We report that two vesicular proteins , Snapin and synaptotagmin 9 ( Syt 9 ) , strongly interact in vitro and in vivo with the TRPV 1 N terminal domain . ^^^ In primary dorsal root ganglion neurons , TRPV 1 co distributes in vesicles with Syt 9 and the vesicular protein synaptobrevin . ^^^ Neither Snapin nor Syt 9 affected channel function , but they notably inhibited protein kinase C ( PKC ) induced potentiation of TRPV 1 channel activity with a potency that rivaled the blockade evoked by botulinum neurotoxin A , a potent blocker of neuronal exocytosis . ^^^ |