Expression and characterization of human PDEδ and its Caenorhabditis elegans ortholog CEδ

FEBS Letters

Li, Ning¹  Baehr, Wolfgang¹ 

[1] Moran Eye Center, University of Utah Health Science Center, 75 N. Medical Dr., Salt Lake City, UT 84132, USA

关键词: Phototransduction;    Membrane attachment;    cGMP phosphodiesterase;    Mammalian retina;    Caenorhabditis elegans C27H5.1 gene product;   

DOI  :  10.1016/S0014-5793(98)01501-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown