Evidence for Functional Diversity between the Voltage-Gated Proton Channel Hv1 and Its Closest Related Protein HVRP1

摘要: The Hv1 channel and voltage-sensitive phosphatases share with voltage-gated sodium, potassium, calcium channels the ability to detect changes in membrane potential through voltage-sensing domains (VSDs). However, they lack pore domain typical of these other channels. NaV, KV, CaV proteins can be found neurons muscles, where play important roles electrical excitability. In contrast, VSD-containing lacking a are non-excitable cells not involved neuronal signaling. Here, we report identification HVRP1, protein related (from which name Related Protein 1 is derived), find expressed primarily central nervous system, particularly cerebellum. Within cerebellar tissue, HVRP1 specifically granule neurons, as determined by situ hybridization immunohistochemistry. Analysis subcellular distribution via electron microscopy immunogold labeling reveals that localizes on post-synaptic side contacts between glutamatergic mossy fibers cells. We also that, despite similarities amino acid sequence structural organization two have distinct functional properties. high conservation vertebrates its cellular localizations suggest an function system.