Expression and characterization of human PDEdelta and its Caenorhabditis elegans ortholog CEdelta.
FEBS Lett
; 440(3): 454-7, 1998 Dec 04.
Article
en En
| MEDLINE
| ID: mdl-9872421
ABSTRACT
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.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas del Helminto
/
Caenorhabditis elegans
/
3',5'-GMP Cíclico Fosfodiesterasas
/
Proteínas del Ojo
Límite:
Animals
/
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
1998
Tipo del documento:
Article
País de afiliación:
Estados Unidos