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.
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1 August 1993
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August 01 1993
Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis
JA Porter,
JA Porter
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
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C Montell
C Montell
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
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JA Porter
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
C Montell
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1993) 122 (3): 601–612.
Citation
JA Porter, C Montell; Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis. J Cell Biol 1 August 1993; 122 (3): 601–612. doi: https://doi.org/10.1083/jcb.122.3.601
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