Expression and characterization of human PDEδ and itsCaenorhabditiselegansortholog CEδ

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Abstract
Cyclic GMP phosphodiesterase (PDE) is rod photoreceptor disk membrane-associated via C-terminal lipid tails. PDEδ, a recently identified subunit, was shown to disrupt PDE/membrane interaction under physiological conditions, without affecting PDE catalytic activity. We found that a PDEδ ortholog from the eyeless nematode Caenorhabditis elegans (termed CEδ) solubilizes bovine PDE in vitro with an EC50 very similar to PDEδ. Immobilized PDEδ and CEδ both bind, in addition to bovine PDE, an N-terminal fragment of human retinitis pigmentosa GTPase regulator, but not rhodopsin kinase and Ran binding protein 1. The results suggest that PDEδ and CEδ may regulate membrane binding of a variety of proteins in photoreceptors and other tissues