Endoplasmic reticulum- plasma membrane (ER-PM) junctions are important aspects of the cellular structure characterised by close apposition between areas of the ER and PM (<30nm). These structures have many important functions including lipid transfer, protein transport, vesicle trafficking and also serving as multiplex signalling hubs. The latter property is indeed an extremely important aspect of signalling paradigms in excitable cells such as sensory neurons. In such cells, it has previously been shown that various signalling processes, such as G-protein coupled receptor mediated Anoctamin 1 (ANO1) channel activation or store-operated Ca2+ entry (SOCE), readily occur at ER-PM junctions and play an important role in inflammatory signalling. In order to understand junctional signalling, an important question needs to be addressed: which proteins are involved in formation and maintenance of these junctions in sensory neurons. Recently, we identified the junctophilin family of proteins as being important for ER-PM formation and SOCE as part of the inflammatory process in sensory neurons. Another set of proteins, that have been shown to play a role in ER-PM formation in various types of cells, are the Extended Synaptotagmin (Esyt) family of proteins. Interestingly, Esyt1 is activated by Ca2+ and is able to allow ER-PM proximity in a dynamic manner. Using immunohistochemistry we identified high expression levels of Esyt1 in rat dorsal root and trigeminal ganglion neurons (DRG, TG), with expression prevailing in mainly small-diameter neurons. Performed proximity ligation assay demonstrated close proximity between Esyt1, ANO1 or inositol trisphosphate receptors (IP3Rs). In control conditions, there was baseline proximity detected between both Esyt1-ANO1 (1.62 ± 0.136 puncta per cell, n=65 neurons) and Esyt1-IP3R (21.0 ± 2.68 puncta per cell, n=82 neurons). Interestingly, upon application of an inflammatory mediator, bradykinin, there was an increase in the incidence of proximity between Esyt1-ANO1 (11.2 ± 1.29 puncta per cell, p<0.0001, n=93 neurons) however, a significant decrease in the number of Esyt1-IP3R proximity was also detected (7.41 ± 0.678 puncta per cell, p<0.001, n=75 neurons). Furthermore, live cell total internal reflection fluorescence (TIRF) imaging revealed that in DRG overexpressing an Esyt1-GFP protein, application of bradykinin was able to increase TIRF fluorescence (0.11 ± 0.02 ΔF/F0, n=6) suggesting that either there was movement of the ER to the PM upon stimulation or that Esyt1-GFP translocates closer to the PM within the existing ER-PM junctions. We also detected similar signals upon removal of extracellular Ca2+ (0.068 ± 0.0068 ΔF/F0, n=6), suggesting that Esyt1 translocation or ER-PM proximity can be effectively triggered by Ca2+ release from the ER. These data suggest that Esyt1 may be playing an active role in bradykinin-induced inflammatory signalling in sensory neurons and could be important for inflammatory pain generation.