Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis

TitleDistinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis
Publication TypeJournal Article
Year of Publication1993
AuthorsPorter JA, Montell C
JournalJ Cell Biol
Volume122
Pagination601-12
Date Published1993 Aug
ISSN0021-9525
KeywordsAlleles, Amino Acid Sequence, Animals, Base Sequence, Drosophila, Drosophila Proteins, Electroretinography, Eye Proteins, Molecular Sequence Data, Mutagenesis, Site-Directed, Myosin Heavy Chains, Myosins, Phenotype, Photoreceptor Cells, Point Mutation, Protein Kinases, Temperature, Transfection
Abstract

The Drosophila ninaC locus encodes a rhabdomere specific protein (p174) with linked protein kinase and myosin domains, required for a wild-type ERG and to prevent retinal degeneration. To investigate the role for linked kinase and myosin domains, we analyzed mutants generated by site-directed mutagenesis. Mutation of the kinase domain resulted in an ERG phenotype but no retinal degeneration. Deletion of the myosin domain caused a change in the subcellular distribution of p174 and resulted in both ERG and retinal degeneration phenotypes. Temperature-sensitive mutations in the myosin domain resulted in retinal degeneration, but no ERG phenotype. These results indicated that the ERG and retinal degeneration phenotypes were not strictly coupled suggesting that the myosin domain has multiple functions. We propose that the role of the kinase domain is to regulate other rhabdomeric proteins important in phototransduction and that the myosin domain has at least two roles: to traffic the kinase into the rhabdomeres and to maintain the rhabdomeres.

Alternate JournalJ. Cell Biol.
PubMed ID8335687
PubMed Central IDPMC2119665
Grant ListEY08117 / EY / NEI NIH HHS / United States