Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha (PDE6C)

Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha (PDE6C) is an essential enzyme in cone photoreceptor cells, catalyzing the hydrolysis of cGMP during phototransduction and thus playing a vital role in the biochemical cascade responsible for daylight and color vision[1][2][3]. PDE6C forms a homodimer, each monomer regulated by an inhibitory γ-subunit (PDE6H); light-activated visual signaling relieves this inhibition, enabling cGMP hydrolysis and subsequent closure of cGMP-gated channels to trigger the neural response to light[1][2]. Mutations in the PDE6C gene cause inherited cone dystrophies including achromatopsia and cone dystrophy type 4, leading to impaired cone cell function or degeneration[3]. PDE6C is highly specific to cone cells in the retina and is not currently a direct therapeutic drug target, but its genetic and functional importance make it a key molecule both for understanding retinal diseases and as a biomarker in inherited retinal disorders[2][3].

Other names

Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'PDE6CPDEA2ACHM5COD4cGMP phosphodiesterase 6CCone photoreceptor phosphodiesterasecone cGMP phosphodiesterasephosphodiesterase 6C, cGMP-specific, cone, alpha prime

Inhibitors would be expected to block cGMP hydrolysis (though no selective therapeutic inhibitor is in clinical use)