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Science 12 November 1993:
Vol. 262. no. 5136, pp. 1038 - 1042
DOI: 10.1126/science.8235618
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Articles

Science, Vol 262, Issue 5136, 1038-1042
Copyright © 1993 by American Association for the Advancement of Science

articles

Dependence of calmodulin localization in the retina on the NINAC unconventional myosin

JA Porter, M Yu, SK Doberstein, TD Pollard, and C Montell

Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

Calmodulin is a highly conserved regulatory protein found in all eukaryotic organisms which mediates a variety of calcium ion-dependent signalling pathways. In the Drosophila retina, calmodulin was concentrated in the photoreceptor cell microvillar structure, the rhabdomere, and was found in lower amounts in the sub-rhabdomeral cytoplasm. This calmodulin localization was dependent on the NINAC (neither inactivation nor afterpotential C) unconventional myosins. Mutant flies lacking the rhabdomere-specific p174 NINAC protein did not concentrate calmodulin in the rhabdomere, whereas flies lacking the sub-rhabdomeral p132 isoform had no detectable cytoplasmic calmodulin. Furthermore, a defect in vision resulted when calmodulin was not concentrated in the rhabdomeres, suggesting a role for calmodulin in the regulation of fly phototransduction. A general function of unconventional myosins may be to control the subcellular distribution of calmodulin.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)