Requirement for the NINAC kinase/myosin for stable termination of the visual cascade

TitleRequirement for the NINAC kinase/myosin for stable termination of the visual cascade
Publication TypeJournal Article
Year of Publication1998
AuthorsLi HS, Porter JA, Montell C
JournalJ Neurosci
Volume18
Pagination9601-6
Date Published1998 Dec 1
ISSN0270-6474
KeywordsAnimals, Blotting, Western, Calcium, Drosophila, Drosophila Proteins, Eye Proteins, Feedback, Gene Expression Regulation, Enzymologic, Light Signal Transduction, Myosin Heavy Chains, Organisms, Genetically Modified, Phosphorylation, Protein Kinase C, Protein Structure, Tertiary
Abstract

Activation of the Drosophila photoresponse is a rapid process that results in plasma membrane Ca2+ and Na+ conductances. Ca2+ functions in negative feedback regulation of Drosophila vision including deactivation. Protein kinase C (PKC) binds directly to Ca2+ and is required for deactivation. However, the consequences of disrupting phosphorylation of any individual PKC substrate in the Drosophila retina have not been addressed. In the current work, we show that NINAC p174, which consists of a protein kinase domain joined to the head region of myosin heavy chain, is a phosphoprotein and is phosphorylated in vitro by PKC. Mutation of either of two PKC sites in the p174 tail resulted in an unusual defect in deactivation that had not been detected previously for other ninaC alleles or other loci. After cessation of the light stimulus, there appeared to be a transient reactivation of the visual cascade. This phenotype suggests that a mechanism exists to prevent reactivation of the visual cascade and that p174 participates in this process.

Alternate JournalJ. Neurosci.
PubMed ID9822721
Grant ListEY08117 / EY / NEI NIH HHS / United States