MOLECULAR-CLONING AND CHARACTERIZATION OF RETINAL PHOTORECEPTOR GUANYLYL CYCLASE-ACTIVATING PROTEIN

Citation
K. Palczewski et al., MOLECULAR-CLONING AND CHARACTERIZATION OF RETINAL PHOTORECEPTOR GUANYLYL CYCLASE-ACTIVATING PROTEIN, Neuron, 13(2), 1994, pp. 395-404
Citations number
44
Categorie Soggetti
Neurosciences
Journal title
NeuronACNP
ISSN journal
08966273
Volume
13
Issue
2
Year of publication
1994
Pages
395 - 404
Database
ISI
SICI code
0896-6273(1994)13:2<395:MACORP>2.0.ZU;2-A
Abstract
Guanylyl cyclase-activating protein (GCAP) is thought to mediate Ca2+- sensitive regulation of guanylyl cyclase (GC), a key event in recovery of the dark state of rod photoreceptors following light exposure. Her e, we characterize GCAP from several vertebrate species by molecular c loning and provide evidence that GCAP contains a heterogeneously acyla ted N-terminal region that interacts with GC. Vertebrate GCAPs consist of 201-205 amino acids, and sequence analysis indicates the presence of three EF hand Ca2+-binding motifs. These results establish that GCA P is a novel photoreceptor-specific member of a large family of Ca2+-b inding proteins and suggest that it participates in the Ca2+-sensitive activation of GC.