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The Journal of Neuroscience, June 15, 1998, 18(12):4548-4559
A Myosin III from Limulus Eyes Is a
Clock-Regulated Phosphoprotein
Barbara-Anne
Battelle1,
Anne W.
Andrews1,
Bruce G.
Calman1,
James R.
Sellers2,
Robert M.
Greenberg1, and
W. Clay
Smith1
1 Whitney Laboratory and Department of Neuroscience,
University of Florida, St. Augustine, Florida 32086, and
2 Laboratory of Molecular Cardiology, National Heart, Lung,
and Blood Institute, National Institutes of Health, Bethesda,
Maryland 20892-1762
The lateral eyes of the horseshoe crab Limulus
polyphemus undergo dramatic daily changes in structure and
function that lead to enhanced retinal sensitivity and responsiveness
to light at night. These changes are controlled by a circadian neural
input that alters photoreceptor and pigment cell shape, pigment
migration, and phototransduction. Clock input to the eyes also
regulates photomechanical movements within photoreceptors, including
membrane shedding. The biochemical mechanisms underlying these diverse effects of the clock on the retina are unknown, but a major biochemical consequence of activating clock input to the eyes is a rise in the
concentration of cAMP in photoreceptors and the phosphorylation of a
122 kDa visual system-specific protein. We have cloned and sequenced
cDNA encoding the clock-regulated 122 kDa phosphoprotein and show here
that it is a new member of the myosin III family. We report that
Limulus myosin III is similar to other unconventional myosins in that it binds to calmodulin in the absence of
Ca2+; it is novel in that it is phosphorylated
within its myosin globular head, probably by cAMP-dependent protein
kinase. The protein is present throughout the photoreceptor, including
the region occupied by the photosensitive rhabdom. We propose that the
phosphorylation of Limulus myosin III is involved in one
or more of the structural and functional changes that occur in
Limulus eyes in response to clock input.
Key words:
myosin III; ninaC; Limulus
polyphemus; photoreceptor cells; circadian rhythms; octopamine; unconventional myosin; cytoskeleton; Drosophila
melanogaster; cAMP-dependent phosphorylation
Copyright © 1998 Society for Neuroscience 0270-6474/98/18124548-12$05.00/0
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