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Gene Review

ninaC  -  neither inactivation nor afterpotential C

Drosophila melanogaster

Synonyms: 2.2, CG 5125, CG5125, CG54125, CT16120, ...
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Disease relevance of ninaC

  • In the current report, we demonstrate that the ninaC mutation results in light- and age-dependent retinal degeneration [1].
  • The kinase homologous domain (MYOIIIPK) of myosin III was expressed in the baculovirus expression system and purified to homogeneity [2].
  • The genome of each of these viruses consists of two segments of double-stranded RNA (molecular weight range between 2.6 x 10(6) and 2.2 x 10(6), and the virion, capsid proteins fall into three size class categories (large, medium, and small; ranging from 100,000 to 27,000) as determined by polyacrylamide slab gel electrophoresis [3].
  • There were two instances in which homozygosis for the second chromosome caused sterility in both sexes, which was close to the number expected (2.2) on a random basis of 0.0092 S 0.183 X 131 [4].

High impact information on ninaC

  • The Drosophila ninaC locus encodes two photoreceptor cell specific proteins with domains homologous to protein kinases and the myosin heavy chain head [5].
  • We show that the ninaC gene, originally isolated as a Drosophila visual mutation with an electrophysiological phenotype, encodes two novel cytoskeletal proteins [5].
  • We identified the DNA sequences encoding the ninaC gene by rescuing the electrophysiological phenotype using P-element-mediated germ line transformation [5].
  • This calmodulin localization was dependent on the NINAC (neither inactivation nor afterpotential C) unconventional myosins [6].
  • Disruption of the NINAC/INAD interaction delayed termination of the photoreceptor response [7].

Biological context of ninaC


Anatomical context of ninaC

  • Light-dependent subcellular translocation of Gqalpha in Drosophila photoreceptors is facilitated by the photoreceptor-specific myosin III NINAC [12].
  • Ultrastructural studies show that the polypeptides encoded by ninaC are very likely to be important components of the cytoskeletal structure of rhabdomeral microvilli [13].
  • The Drosophila ninaC mutation produces small rhabdomeres with the axial filament of the microvillar cytoskeleton reduced or missing [14].
  • Myosin III immunoreactivity in trilobite larvae also revealed the architecture of the central visual pathways associated with the median eye complex and the lateral eyes [15].
  • The gamma-tubulin ring complex (gammaTuRC) is a protein complex of relative molecular mass approximately 2.2 x 10(6) that nucleates microtubules at the centrosome [16].

Associations of ninaC with chemical compounds

  • To address the requirements for calmodulin binding at each site in vivo, we generated transgenic flies expressing ninaC genes deleted for either C1 or C2 [17].
  • The phosphoamino acid analysis revealed that myosin III is a serine/threonine kinase but not a tyrosine kinase [2].
  • Double labeling with myosin III and BrdU showed that neurogenesis persists in the larval brain and suggested that new neurons of both the lamina and the medulla originate from a single common proliferation zone [15].
  • Polyadenylic acid-containing transcripts of 2.7, 2.2, and 1.7 kilobases (kb) in embryos, pupae, adults, and Kc cells and an additional 1.4-kb transcript in adults were complementary to the Drosophila genomic clones and to v-myc [18].
  • Within the 2.2 kb region between hsp23 and gene 1 of the small heat shock gene locus 67B1 of Drosophila melanogaster, an approximately 1 kb perturbation of the chromatin architecture has previously been observed to occur in response to the steroid hormone ecdysone [19].

Physical interactions of ninaC

  • Biochemical studies showed that both ninaC proteins bind actin filaments and cosediment with actin filaments in an ATP-sensitive manner [20].

Other interactions of ninaC

  • These results outline structural roles for the ninaC proteins, and are consistent with the notion, suggested by their amino acid sequences, that the proteins are actin-based mechanoenzymes [20].
  • MYOIIIPK phosphorylated a number of proteins including myosin III p132 and smooth muscle myosin regulatory light chain (LC20), suggesting that myosin III is a multifunctional protein kinase [2].

Analytical, diagnostic and therapeutic context of ninaC

  • We have: (1) determined the cellular and subcellular distributions of the ninaC proteins in the Drosophila retina by electron microscopic immunocytochemistry with an antibody specific for epitopes shared by both proteins; (2) characterized the ultrastructure of the mutant phenotype [21].
  • The role of p132 and p174 was studied via whole-cell recording and through measurements of the pupil mechanism, i.e. the pigment migration in the photoreceptor cells, in the ninaC mutants, P[ninaC delta 132] (p132 absent), P[ninaC delta 174] (p174 absent), and ninaCP235 (null mutant) [22].
  • Two RNAs of 7.4 and 2.2 kb have been identified by Northern blot analysis as the putative eyecolor and segregational products [23].
  • To understand structural features of the Drosophila PIMT (dPIMT) important for catalysis, the crystal structure of dPIMT was determined at a resolution of 2.2 A, and site-directed mutagenesis was used to identify the role of Ser-60 in catalysis [24].
  • Sequence analysis of the nucleotides spanning the region between 1.3 kb and 2.2 kb revealed a 13-nucleotide motif ACACAAAAAAATA 2059 bp upstream from the start site that duplicated the 'hunchback' binding site, a key site controlling developmental gene expression in Drosophila [25].


  1. Differential localizations of and requirements for the two Drosophila ninaC kinase/myosins in photoreceptor cells. Porter, J.A., Hicks, J.L., Williams, D.S., Montell, C. J. Cell Biol. (1992) [Pubmed]
  2. Identification of myosin III as a protein kinase. Ng, K.P., Kambara, T., Matsuura, M., Burke, M., Ikebe, M. Biochemistry (1996) [Pubmed]
  3. Biophysical and biochemical characterization of five animal viruses with bisegmented double-stranded RNA genomes. Dobos, P., Hill, B.J., Hallett, R., Kells, D.T., Becht, H., Teninges, D. J. Virol. (1979) [Pubmed]
  4. Genes affecting productivity in natural populations of Drosophila melanogaster. Watanabe, T.K., Onishi, S. Genetics (1975) [Pubmed]
  5. The Drosophila ninaC locus encodes two photoreceptor cell specific proteins with domains homologous to protein kinases and the myosin heavy chain head. Montell, C., Rubin, G.M. Cell (1988) [Pubmed]
  6. Dependence of calmodulin localization in the retina on the NINAC unconventional myosin. Porter, J.A., Yu, M., Doberstein, S.K., Pollard, T.D., Montell, C. Science (1993) [Pubmed]
  7. Termination of phototransduction requires binding of the NINAC myosin III and the PDZ protein INAD. Wes, P.D., Xu, X.Z., Li, H.S., Chien, F., Doberstein, S.K., Montell, C. Nat. Neurosci. (1999) [Pubmed]
  8. Light-dependent translocation of visual arrestin regulated by the NINAC myosin III. Lee, S.J., Montell, C. Neuron (2004) [Pubmed]
  9. Subcellular translocation of the eGFP-tagged TRPL channel in Drosophila photoreceptors requires activation of the phototransduction cascade. Meyer, N.E., Joel-Almagor, T., Frechter, S., Minke, B., Huber, A. J. Cell. Sci. (2006) [Pubmed]
  10. Modulation of the light response by cAMP in Drosophila photoreceptors. Chyb, S., Hevers, W., Forte, M., Wolfgang, W.J., Selinger, Z., Hardie, R.C. J. Neurosci. (1999) [Pubmed]
  11. Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis. Porter, J.A., Montell, C. J. Cell Biol. (1993) [Pubmed]
  12. Light-dependent subcellular translocation of Gqalpha in Drosophila photoreceptors is facilitated by the photoreceptor-specific myosin III NINAC. Cronin, M.A., Diao, F., Tsunoda, S. J. Cell. Sci. (2004) [Pubmed]
  13. Gene encoding cytoskeletal proteins in Drosophila rhabdomeres. Matsumoto, H., Isono, K., Pye, Q., Pak, W.L. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  14. Anti-actin immunoreactivity is retained in rhabdoms of Drosophila ninaC photoreceptors. Stowe, S., Davis, D.T. Cell Tissue Res. (1990) [Pubmed]
  15. Evolution of arthropod visual systems: Development of the eyes and central visual pathways in the horseshoe crab Limulus polyphemus Linnaeus, 1758 (Chelicerata, Xiphosura). Harzsch, S., Vilpoux, K., Blackburn, D.C., Platchetzki, D., Brown, N.L., Melzer, R., Kempler, K.E., Battelle, B.A. Dev. Dyn. (2006) [Pubmed]
  16. Structure of the gamma-tubulin ring complex: a template for microtubule nucleation. Moritz, M., Braunfeld, M.B., Guénebaut, V., Heuser, J., Agard, D.A. Nat. Cell Biol. (2000) [Pubmed]
  17. Calmodulin binding to Drosophila NinaC required for termination of phototransduction. Porter, J.A., Minke, B., Montell, C. EMBO J. (1995) [Pubmed]
  18. Family of developmentally regulated, maternally expressed Drosophila RNA species detected by a v-myc probe. Madhavan, K., Bilodeau-Wentworth, D., Wadsworth, S.C. Mol. Cell. Biol. (1985) [Pubmed]
  19. Multiple interacting elements delineate an ecdysone-dependent regulatory region with secondary responsive character. Rogulski, K.R., Cartwright, I.L. J. Mol. Biol. (1995) [Pubmed]
  20. Role of the ninaC proteins in photoreceptor cell structure: ultrastructure of ninaC deletion mutants and binding to actin filaments. Hicks, J.L., Liu, X., Williams, D.S. Cell Motil. Cytoskeleton (1996) [Pubmed]
  21. Distribution of the myosin I-like ninaC proteins in the Drosophila retina and ultrastructural analysis of mutant phenotypes. Hicks, J.L., Williams, D.S. J. Cell. Sci. (1992) [Pubmed]
  22. Differential effects of ninaC proteins (p132 and p174) on light-activated currents and pupil mechanism in Drosophila photoreceptors. Hofstee, C.A., Henderson, S., Hardie, R.C., Stavenga, D.G. Vis. Neurosci. (1996) [Pubmed]
  23. The claret locus in Drosophila encodes products required for eyecolor and for meiotic chromosome segregation. Yamamoto, A.H., Komma, D.J., Shaffer, C.D., Pirrotta, V., Endow, S.A. EMBO J. (1989) [Pubmed]
  24. Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis. Bennett, E.J., Bjerregaard, J., Knapp, J.E., Chavous, D.A., Friedman, A.M., Royer, W.E., O'Connor, C.M. Biochemistry (2003) [Pubmed]
  25. Pretranslational control of Menkes disease gene expression. Harris, E.D., Reddy, M.C., Majumdar, S., Cantera, M. Biometals (2003) [Pubmed]
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