| Literature DB >> 12596915 |
Satoru Kawamura1, Shuji Tachibanaki.
Abstract
S-Modulin is a Ca2+-binding protein found in frog rod photoreceptors (1,2) and its bovine homologue is known as recoverin (3,4). In the Ca2+-bound form, S-modulin inhibits rhodopsin phosphorylation5 through inhibition of rhodopsin kinase. (6-9) Because rhodopsin phosphorylation is the quench mechanism of light-activated rhodopsin (R*), (10,11) the inhibition of the phosphorylation by S-modulin probably contributes to increase the lifetime of R* to result in sustained hydrolysis of cGMP5. The Ca2+ concentration decreases in the light in vertebrate photoreceptors, (12-14) and this decrease is essential for light-adaptation. (15,16) Thus, S-modulin is expected to regulate the lifetime of R* and thereby regulate the extent and the time course of hydrolysis of cGMP depending on the intensity of background light. With this mechanism, S-modulin is believed to regulate the waveform of a photoresponse and the efficiency of the light in the generation of a photoresponse.Entities:
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Year: 2002 PMID: 12596915 DOI: 10.1007/978-1-4615-0121-3_4
Source DB: PubMed Journal: Adv Exp Med Biol ISSN: 0065-2598 Impact factor: 2.622