Abstract

Rhodopsin absorbs light and undergoes a photobleaching. Its intermediates activate a cGMP cascade that generates a hyperpolarized potential in rod photoreceptor cells. This light-triggered cascade reaction is terminated and completely restored to the dark levels by another enzymatically controlled reaction initiated by rhodopsin phosphorylation by rhodopsin kinase. Thus, phosphorylation and dephosphorylation of rhodopsin is a crucial regulatory mechanism of photoreception of rods. I found that rhodopsin phosphorylation predominantly occurs at 334, 338 and 343 serine residues in both in vivo and in vitro. Furthermore, I also found rhodopsin phosphorylation is involved in not only the quenching phototransduction but the dark adaptation processes.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.