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Visual arrestin in Limulus is phosphorylated at multiple sites in the light and in the dark

Published online by Cambridge University Press:  15 December 2000

B-A. BATTELLE ,
A.W. ANDREWS ,
K.E. KEMPLER ,
S.C. EDWARDS  and
W.C. SMITH
B-A. BATTELLE
Affiliation:
Whitney Laboratory and Department of Neuroscience, University of Florida, St. Augustine
A.W. ANDREWS
Affiliation:
Whitney Laboratory and Department of Neuroscience, University of Florida, St. Augustine
K.E. KEMPLER
Affiliation:
Whitney Laboratory and Department of Neuroscience, University of Florida, St. Augustine
S.C. EDWARDS
Affiliation:
Department of Pharmacology and Experimental Therapeutics, University of South Florida, Tampa
W.C. SMITH
Affiliation:
Whitney Laboratory and Department of Neuroscience, University of Florida, St. Augustine Department of Ophthalmology, University of Florida, Gainesville
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Abstract

Arrestins participate in the termination of phototransduction in both vertebrates and invertebrates. However, the visual arrestins of invertebrates and vertebrates differ significantly from one another in that the invertebrate visual arrestins become phosphorylated rapidly in response to light while those in the photoreceptors of vertebrates do not. In an effort to understand the functional relevance of arrestin phosphorylation, we examined this process in the photoreceptors of the horseshoe crab Limulus polyphemus. We report that Limulus visual arrestin can be phosphorylated at three sites near its C-terminus and show that arrestin molecules phosphorylated on one, two, and three sites are normally present in both light- and dark-adapted photoreceptors. Light adaptation increases the amount of arrestin phosphorylated at three sites.

Keywords

ArrestinPhotoreceptorsPhototransductionLimulusCalcium/calmodulin-dependent protein kinase IIS-antigen
Type
Research Article
Information
Visual Neuroscience , Volume 17 , Issue 5 , September 2000 , pp. 813 - 822
Copyright
2000 Cambridge University Press

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