Transient receptor potential cation channel subfamily V (for vanilloid) subtype 2 (TRPV2 for short, from "transient receptor potential cation channel subfamily V member 2") is a calcium-permeable cation channel expressed in sensory neurons of the vertebrate central and peripheral nervous systems. TRPV2, unlike TRPV1, is expressed in medium to large neurons of the spinal cord, brain, and motor neurons. (TRPV2 and TRPV1 share 50% sequence identity). TRPV2 was initially characterized as a noxious heat sensor, but it also has mechanosensory properties (Aguettaz E et al. 2017; Shibasaki K 2016).
TRP channels are phylogenetically early signaling pathways (they can be detected as early as yeast cells). The first TRP channel was identified in 1989 in the context of visual perception in Drosophila melanogaster. In a Drosophila mutant (trp343), it was shown that its photoreceptors responded to light stimuli only with a transient, i.e. rapidly inactivating, membrane current. In the non-mutated wild type, however, the current flow persisted as long as light hit the photoreceptor. The mutant protein -TRP- was cloned in 1989. Thus, the name "transient receptor potential" - TRP- refers to the description of a phenotype of a mutant of the fruit fly Drosophila melanogaster. TRP channels exert important functions in primary signaling pathways for the regulated influx of Ca2+ into a cell in both vertebrates and non-vertebrates. TRP channels in humans play an important role in the sensation of different types of taste (sweet, bitter, umami) as well as in the perception of pain, heat, warmth or cold, pressure and light. It is believed that some TRP channels in the body behave like microscopic thermosensors. So far, 28 TRP channel genes have been identified in mammals (Nilius B et al. 2011).