The next few questions will relate to this passage and figure.
The structure of the TRPV1 protein consists of several transmembrane domains that are embedded in the membrane as well as a carboxy-terminus and an amino-terminus that are located inside the cell. TRPV1 is activated by several stimuli, including the binding of capsaicin, a chemical found in chili peppers. Capsaicin enters the cell by simple diffusion and then binds to one of the transmembrane domains of TRPV1, which opens the ion channel. The opening of the TRPV1 channel allows Ca²⁺ ions to enter the cell, leading to the activation of the enzyme calcineurin. Calcineurin removes phosphate groups from the phosphorylated form of the transcription factor NFAT2, which is typically found in the cytoplasm. Once dephosphorylated, NFAT2 moves into the nucleus, where it blocks the transcription of another protein, ATF3. ATF3, when active, prevents the cell cycle regulatory protein pGoG from inducing apoptosis and blocking cell division (see figure). Low extracellular pH activates TRPV1 through the binding of H⁺ ions to TRPV1.