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ATP-independent deactivation of squid rhodopsin

Published online by Cambridge University Press:  02 June 2009

Alon Kahana ,
Phyllis R. Robinson ,
Laura J. Lewis ,
Ete Z. Szuts  and
John E. Lisman
Alon Kahana
Affiliation:
Department of Biology, The Center for Complex Systems, Brandeis University, Waltham and Marine Biological Laboratory, Woods Hole
Phyllis R. Robinson
Affiliation:
Department of Biology, The Center for Complex Systems, Brandeis University, Waltham and Marine Biological Laboratory, Woods Hole
Laura J. Lewis
Affiliation:
Department of Biology, The Center for Complex Systems, Brandeis University, Waltham and Marine Biological Laboratory, Woods Hole
Ete Z. Szuts
Affiliation:
Department of Biology, The Center for Complex Systems, Brandeis University, Waltham and Marine Biological Laboratory, Woods Hole
John E. Lisman
Affiliation:
Department of Biology, The Center for Complex Systems, Brandeis University, Waltham and Marine Biological Laboratory, Woods Hole Reprint requests to: John E. Lisman, Department of Biology, The Center for Complex Systems, Brandeis University, Waltham, MA 02254-9110, USA.
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Abstract

Deactivation of light-activated squid rhodopsin was studied in vitro using GTPγS binding by G-protein as a direct measure of rhodopsin activity. Deactivation was inhibited by dilution of the retinal suspension or by removal of soluble components. Deactivation could be restored by addition of soluble material to washed membranes. These results indicate that the deactivation is not due entirely to a conformational transition within rhodopsin itself, but depends on the interaction with other molecules. The possibility that phosphorylation is involved in the deactivation was studied. Deactivation occurred in the presence and absence of added ATP. Deactivation also occurred in the presence of kinase inhibitors and after addition of apyrase, which reduced residual ATP levels to below 1μM. These results indicate that light-induced phosphorylation is not required for deactivation of squid rhodopsin. In this regard deactivation of squid rhodopsin is different from that of vertebrate rhodopsin, which requires phosphorylation.

Keywords

PhosphorylationInactivationArrestinG-proteinRhodopsin kinaseSwitch
Type
Research Article
Information
Visual Neuroscience , Volume 9 , Issue 6 , December 1992 , pp. 595 - 602
Copyright
Copyright © Cambridge University Press 1992

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