ABSTRACT
PDE7A1 proteins have been localized mainly to the outer face of the Golgi apparatus and are distributed throughout the cytoplasm. Human PDE7A3 is a 50 kDa protein of 425 amino acids encoded by a transcript with an uncharacterized 5' end. PDE7B1 has been implicated in negative feedback regulation of dopaminergic signaling in rat striatal neurons through up-regulation of PDE7B1 expression. Knowledge of the PDE7 family of 3',5'-cyclic adenosine monophosphate (cAMP)-specific phosphodiesterases (PDE) has clearly expanded since the discovery of this novel, undetected, family of PDEs, and with it the number of new questions that have arisen. Development of novel drugs, or methods, to inhibit activities or expression of all PDE7A1 domains, is required to block its contribution to cAMP and protein kinase A signaling. The unique N-terminus of PDE7A2 is 20 residues long, is hydrophobic, and confers an association of PDE7A2 with particulate membrane fractions including the plasma membrane.
