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Crozet F, El-Amraoui A, Blanchard S, Lenoir M, Ripoll C, Vago P, Hamel C, Fizames C, Levi-Acobas F, Depetris D et al.: Cloning of the genes encoding two murine and human cochlear unconventional type I myosins. Genomics 1997, 40:332-341.
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Yamoah EN, Gillespie PG: Phosphate analogs block adaptation in hair cells by inhibiting adaptation-motor force production. Neuron 1996, 17:523-533. The Gillespie lab has provided further evidence that the adaptation motor is probably a myosin by showing that inhibitors of myosin ATPase also inhibit adaptation. It is exciting to see that the candidate for the adaptation motor, the 120 kDa myosin isozyme, exhibits similar sensitivities to these inhibitors in photoaffinity labeling studies.
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Yamoah, E.N.1
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Calmodulin controls adaptation of mechanoelectrical transduction by hair cells of the bullfrog's sacculus
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2+-calmodulin. As myosins are associated with calmodulin light chains, this evidence suggests that the sensitivity of adaptation to calmodulin inhibitors is mediated by a myosin.
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Burlacu S, Tap WD, Lumpkin EA, Hudspeth A: ATPase activity of myosin in hair bundles of the bullfrog's sacculus. Biophys J 1997, 72:263-271. This manuscript analyzes the ATPase activity present in isolated hair bundles and finds that adaptation is insensitive to NEM, a potent inhibitor of many myosins. In this exciting manuscript, the authors observe that the candidate for the adaptation motor, the 120 kDa myosin isozyme, appears to be NEM-insensitive during photoaffinity labeling, providing a further connection between this myosin and the adaptation motor.
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Zhu T, Sata M, Ikebe M: Functional expression of mammalian myosin Iβ: analysis of its motor activity. Biochemistry 1996, 35:513-522. This important biochemical analysis of myosin Iβ provides the baseline for a direct comparison of the properties of the adaptation motor and the properties of this unconventional myosin.
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Hasson T, Walsh J, Cable J, Mooseker MS, Brown SDM, Steel KP: Effects of shaker-1 mutations on myosin Vila protein and mRNA expression. Cell Motil Cytoskeleton 1997, 37:127-138. As a first step towards understanding the role of myosin VIIa in disease, these authors have characterized myosin expression in the mouse mutant shaker-1. Here, they present data that the retinal and testicular morphology of these mutants is similar to wild-type, an unexpected result given the high level of expression of myosin VIIa in these tissues. Also, the expression profile of myosin Vila is found to vary widely among the various shaker-1 alleles, suggesting that small mutations may have drastic effects on myosin Vila protein stability.
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Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis
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Porter JA, Montell C: Distinct roles of the Drosophila ninaC kinase and myosin domains revealed by systematic mutagenesis. J Cell Biol 1993, 122:601-612.
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Dependence of calmodulin localization in the retina on the NINAC unconventional myosin
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Porter JA, Yu M, Doberstein SK, Pollard TD, Montell C: Dependence of calmodulin localization in the retina on the NINAC unconventional myosin. Science 1993, 262:1038-1042.
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Role of the NinaC proteins in photoreceptor cell structure: Ultrastructure of NinaC deletion mutants and binding to actin filaments
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Hicks JL, Liu X, Williams DS: Role of the NinaC proteins in photoreceptor cell structure: ultrastructure of NinaC deletion mutants and binding to actin filaments. Cell Motil Cytoskeleton 1996, 35:367-379.
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Identification of myosin III as a protein kinase
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Ng KP, Kambara T, Matsuura M, Burke M, Ikebe M: Identification of myosin III as a protein kinase. Biochemistry 1996, 35:9392-9399. The first evidence that the kinase domain found on the amino terminus of NinaC is an active enzyme capable of phosphorylating a number of substrates. This enzymatic analysis confirms the genetic data [51] showing that the kinase serves an essential role in the function of the protein in the retina of Drosophila.
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Human Usher 1b/mouse shaker-1: The retinal phenotype discrepancy explained by the presence/absence of myosin VIIA in the photoreceptor cells
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El-Amraoui A, Sahly I, Picaud S, Sahel J, Abitbol M, Petit C: Human Usher 1b/mouse shaker-1: the retinal phenotype discrepancy explained by the presence/absence of myosin VIIA in the photoreceptor cells. Hum Mol Genet 1996, 5:1171-1178. This important immunolocalization study shows that myosin Vila is expressed in both the pigmented epithelium and the photoreceptors of the human eye. This contrasts with earlier work, which had located myosin VIIa only to the pigmented epithelium in rodents [34]. The authors suggest that this expression profile explains the phenotypic differences observed between shaker-1 mice and Usher patients.
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Immunogold localization of myosin in the photoreceptor cilium
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