Abstract
Transient receptor potential (TRP) ion channels are emerging as a new set of membrane proteins involved in a vast array of cellular processes and regulated by a large number of physical and chemical stimuli, which involves them with sensory cell physiology. The vanilloid TRP subfamily (TRPV) named after the vanilloid receptor 1 (TRPV1) consists of six members, and at least four of them (TRPV1-TRPV4) have been related to thermal sensation. One of the least characterized members of the TRP subfamily is TRPV2. Although initially characterized as a noxious heat sensor, TRPV2 now seems to have little to do with temperature sensing but a much more complex physiological profile. Here we review the available information and research progress on the structure, physiology and pharmacology of TRPV2 in an attempt to shed some light on the physiological and pharmacological deorphanization of TRPV2. Here we outline the current knowledge on transient receptor potential vanilloid 2 (TRPV2) ion channel. Although initially described as a noxious heat thermosensor, its molecular mechanism and regulation has been revealed as much more complex and still to be fully elucidated. The present work attempts to highlight the most relevant structural features and physiological roles for TRPV2. © 2013 FEBS.
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Perálvarez-Marín, A., Doñate-Macian, P., & Gaudet, R. (2013). What do we know about the transient receptor potential vanilloid 2 (TRPV2) ion channel? In FEBS Journal (Vol. 280, pp. 5471–5487). https://doi.org/10.1111/febs.12302
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