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PMID: 6279759 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Calcium and cyclic GMP regulation of light-sensitive protein phosphorylation in frog photoreceptor membranes.

The Journal of general physiology ·Vol. 79 ·No. 4 ·1982-04-00 ·Pages 633-55

Hermolin J, Karell MA, Hamm HE, Bownds MD

Abstract

In frog photoreceptor membranes, light induces a dephosphorylation of two small proteins and a phosphorylation of rhodopsin. The level of phosphorylation of the two small proteins is influenced by cyclic GMP. Measurement of their phosphorylation as a function of cyclic GMP concentration shows fivefold stimulation as cyclic GMP is increased from 10(-5) to 10(-3) M. This includes the concentration range over which light activation of a cyclic GMP phosphodiesterase causes cyclic GMP levels to fall in vivo. Cyclic AMP does not affect the phosphorylations. Calcium ions inhibit the phosphorylation reactions. Calcium inhibits the cyclic GMP-stimulated phosphorylation of the small proteins as its concentration is increased from 10(-6) to 10(-3) M, with maximal inhibition of 70% being observed. Rhodopsin phosphorylation is not stimulated by cyclic nucleotides, but is inhibited by calcium, with 50% inhibition being observed as the Ca++ concentration is increased from 10(-9) to 10(-3) M. A nucleotide binding site appears to regulate rhodopsin phosphorylation. Several properties of the rhodopsin phosphorylation suggest that it does not play a role in a rapid ATP-dependent regulation of the cyclic GMP pathway. Calcium inhibition of protein phosphorylation is a distinctive feature of this system, and it is suggested that Ca++ regulation of protein phosphorylation plays a role in the visual adaptation process. Furthermore, the data provide support for the idea that calcium and cyclic GMP pathways interact in regulating the light-sensitive conductance.

MeSH Terms
Animals Calcium/physiology Chemistry, Organic Cyclic GMP/physiology Eye Proteins/metabolism Light Membranes/metabolism Organic Chemistry Phenomena Phosphorylation Photoreceptor Cells/metabolism,ultrastructure Rana catesbeiana Ranidae Rhodopsin/metabolism Time Factors
Chemicals
Eye Proteins Rhodopsin Cyclic GMP Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hermolin J
Karell M A
Hamm H E
Bownds M D
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Article Info
Journal
The Journal of general physiology
Abbr.
J Gen Physiol
ISSN
0022-1295
Published
1982-04-00
Pages
633-55
Language
English
Region
United States
NLM ID
2985110R
PMCID
PMC2215482
Subset
IM
Grants
NEI NIH HHS · 1-T32-EY-07059 · United States
NEI NIH HHS · EY-00463 · United States
OHS HRSA HHS · ST-32-GM-07507 · United States
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