Expression and characterization of human PDEdelta and its Caenorhabditis elegans ortholog CEdelta.
Cyclic GMP phosphodiesterase ( PDE) is rod photoreceptor disk membrane-associated via C-terminal lipid tails. PDEdelta, a recently identified subunit, was shown to disrupt PDE/membrane interaction under physiological conditions, without affecting PDE catalytic activity. We found that a PDEdelta ortholog from the eyeless nematode Caenorhabditis elegans (termed CEdelta) solubilizes bovine PDE in vitro with an EC50 very similar to PDEdelta. Immobilized PDEdelta and CEdelta 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 PDEdelta and CEdelta may regulate membrane binding of a variety of proteins in photoreceptors and other tissues.[1]References
- Expression and characterization of human PDEdelta and its Caenorhabditis elegans ortholog CEdelta. Li, N., Baehr, W. FEBS Lett. (1998) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
