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Article

Calmodulin binding to Drosophila NinaC required for termination of phototransduction.

The EMBO journal - 15 Sept 1995

Porter J A, Minke B, Montell C

Abstract excerpt

The ninaC locus encodes two unconventional myosins, p132 and p174, consisting of fused protein kinase and myosin head domains expressed in Drosophila photoreceptor cells. NinaC are the major calmodulin-binding proteins in the retina and the NinaC-calmodulin interaction is required for the normal subcellular localization of calmodulin as well as for normal photo-transduction. In the current report, we present...

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Identifiers

PMID: 7556088
DOI: 10.1002/j.1460-2075.1995.tb00124.x
PMCID: PMC394537

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Calmodulin binding to Drosophila NinaC required for termination of phototransduction.PMID 7556088Read ↗

Differential localizations of and requirements for the two Drosophila ninaC kinase/myosins in photoreceptor cells.Semantic proximity Read ↗

Role of the ninaC proteins in photoreceptor cell structure: ultrastructure of ninaC deletion mutants and binding to actin filaments.Semantic proximity Read ↗

Dependence of calmodulin localization in the retina on the NINAC unconventional myosin.Semantic proximity Read ↗

Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis.Semantic proximity Read ↗

Distribution of the myosin I-like ninaC proteins in the Drosophila retina and ultrastructural analysis of mutant phenotypes.Semantic proximity Read ↗

Role of Ca2+/calmodulin-dependent protein kinase II in Drosophila photoreceptors.Semantic proximity Read ↗

Calmodulin binds to Drosophila TRP with an unexpected mode.Semantic proximity Read ↗

Photoreceptor degeneration and Ca2+ influx through light-activated channels of Drosophila.Semantic proximity Read ↗

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Ca2+-dependent metarhodopsin inactivation mediated by calmodulin and NINAC myosin III.Semantic proximity Read ↗

PDA (prolonged depolarizing afterpotential)-defective mutants: the story of nina's and ina's--pinta and santa maria, too.Semantic proximity Read ↗

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