Transient receptor potential cation channel subfamily C member 1 (TRPC1) (TRPC1)

The Transient receptor potential cation channel subfamily C member 1 (TRPC1) is a plasma membrane protein that forms receptor-activated non-selective cation channels permeable to Ca2+ and Na+, contributing to store-operated Ca2+ entry and cytosolic Ca2+ elevation upon endoplasmic reticulum Ca2+ release. It typically functions as a heterotetramer, associating with TRPC4, TRPC5, or other TRPC members rather than forming homomers, which alters ion selectivity, rectification properties, and gating compared to homomeric channels. TRPC1 colocalizes with STIM1 and Orai1 at endoplasmic reticulum-plasma membrane junctions to facilitate Ca2+ influx via I_CRAC or I_SOC currents, and it may also contribute to mechanosensitivity, though evidence is conflicting. Structurally, it features six transmembrane helices (S1-S6), a pore loop between S5 and S6, ankyrin repeats in the N-terminus, and motifs like CIRB for regulatory interactions. In physiology, TRPC1 supports processes like fear/stress responses, dopaminergic neuron integrity, and membrane excitability in various tissues. Disease associations include roles in cardiovascular and neurodegenerative conditions, positioning it as a potential therapeutic target, though specific drugs remain underdeveloped. Cryo-EM structures of TRPC1/TRPC4 heteromers reveal asymmetric gates and selectivity filters influencing monovalent cation preference.

Other names

Short transient receptor potential channel 1