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Calcium/calmodulin-stimulated phosphorylation of photoreceptor proteins in Limulus

Published online by Cambridge University Press:  02 June 2009

Eric M. Wiebe
Affiliation:
The Whitney Laboratory and the Department of Neuroscience, University of Florida, St. Augustine
Anne C. Wishart
Affiliation:
The Whitney Laboratory and the Department of Neuroscience, University of Florida, St. Augustine
Samuel C. Edwards
Affiliation:
The Whitney Laboratory and the Department of Neuroscience, University of Florida, St. Augustine
Barbara-Anne Battelle*
Affiliation:
The Whitney Laboratory and the Department of Neuroscience, University of Florida, St. Augustine
*
Correspondence and reprint requests to: Barbara-Anne Battelle, The Whitney Laboratory and the Department of Neuroscience, University of Florida, 9505 Ocean Shore Boulevard, St. Augustine, FL 32086, USA.

Abstract

Calcium (Ca2+) is thought to play a major role in the photoresponse of both vertebrates and invertebrates, but the mechanisms through which Ca2+ exerts its effects are unclear. In many systems, some effects of Ca2+ on cellular processes are thought to be mediated via activation of calcium/calmodulin protein kinase (CaCAM-PK) and the phosphorylation of specific proteins. Thus, protein substrates for CaCAM-PK in photoreceptor cells may be important in mediating the effects of Ca2+ on the photoresponse.

In this study, we identify eight substrates for CaCAM-PK found in both the ventral and lateral eyes of Limulus. We focus on a characterization of one of these, a 46-kD substrate. We show that its subcellular distribution in ventral photoreceptors and its isoelectric forms are identical to the 46-kD light-stimulated phosphoprotein (46A) described by Edwards et al. (1989). Furthermore, we present evidence that 46A is unique to photoreceptor cells, and that it is present throughout the cell. Based on the results of this study, and the previous study by Edwards et al. (1989), we propose that 46A is involved in mediating the effects of Ca2+ on Limulus photoreceptor cell function, and that it may be involved in dark adaptation.

Type
Research Articles
Copyright
Copyright © Cambridge University Press 1989

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