PDE6D Human

PDE6D was originally identified as the fourth subunit of the rod cell-specific cGMP phosphodiesterase (PDE) complex . The PDE6 complex is a heterodimer composed of alpha and beta catalytic subunits, regulated by two inhibitory gamma subunits. PDE6D, however, does not modify the catalytic properties of the PDE alpha-beta dimer .

The precise function of PDE6D within the rod-specific GMP-PDE complex remains somewhat unclear. However, it is known that PDE6D is not confined to photoreceptor cells but is widely distributed in different tissues . It is thought to act as a specific soluble transport factor for certain prenylated proteins and Arl2-GTP, a regulator of PDE-mediated transport .

PDE6D promotes the release of prenylated target proteins from cellular membranes and modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location . It is required for the normal ciliary targeting of farnesylated target proteins, such as INPP5E .

Mutations in the PDE6D gene are associated with Joubert syndrome-22, a rare genetic disorder characterized by developmental delays, ataxia, and other neurological symptoms . Additionally, PDE6D is involved in the regulation of the membrane association of Ras and Rap GTPases, which are important for various cellular processes .

Recombinant human PDE6D is used in research to study its role in phototransduction and its interactions with other proteins. It is also utilized in the development of potential therapeutic interventions for diseases associated with PDE6D dysfunction.