Transient receptor potential cation channel subfamily C member 1 and member 6 (TRPC1 and TRPC6)

TRPC1 and TRPC6 are members of the transient receptor potential canonical (TRPC) subfamily of *nonselective cation channels* that permeate Ca²⁺, Na²⁺, and other cations. Structurally, they form homo- or heterotetramers using six transmembrane domains, with intracellular N- and C-termini that contain regulatory motifs (e.g., ankyrin repeats). TRPC1 and TRPC6 are widely expressed and regulate intracellular calcium dynamics, thereby impacting cellular functions including signal transduction, muscle contraction, neuronal development, and immune responses. Dysfunction or mutations in these channels are implicated in diverse pathologies, particularly cardiovascular and renal diseases. TRPC6, in particular, is activated by diacylglycerol (DAG), and is a validated therapeutic target due to its role in adverse cardiac and renal remodeling. Several small-molecule agonists and antagonists—such as BTDM and Hyperforin—interact with distinct ligand-binding pockets, illustrating druggability. Safety concerns in therapeutic targeting center around potential dysregulation of calcium homeostasis, heart function, and widespread physiological roles of these channels[2][3][5][6].

Other names

Transient receptor potential canonical 1TRP channel protein 1Transient receptor potential canonical 6TRP channel protein 6

Inhibition of TRPC6-mediated cation influx (by BTDM and similar inhibitors)[3][5] Activation of TRPC6 by diacylglycerol (DAG) and some agonists[2][3][5] Modulation of hetero- and homotetramer channel formation, affecting cation permeability[6]