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  • 1
    Electronic Resource
    Electronic Resource
    An altered electroretinogram transient associated with an unusual jump response in a mutant ofDrosophila (1983)
    Springer
    Cellular and molecular neurobiology 3 (1983), S. 143-149 
    Details
    ISSN: 1573-6830
    Keywords: electroretinogram ; visual mutants ; visual sensitization ; Drosophila
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Mutations at thestoned locus ofDrosophila melanogaster produce a reversible temperature-sensitive debilitation. At permissive temperatures they also exhibit an unusual jump response to a light-off stimulus. 2. An increase in the amplitude of the off-transient of the electroretinogram (ERG) is associated with this abnormal jump. Both the jump response and the increased amplitude of the off-transient are shown to be dependent on the duration of the light pulse prior to the light-off stimulus. 3. Instoned flies which are light adapted, the jump response, as measured by recording from the indirect flight muscles, is seen to habituate with increasing light-off frequency. This habituation corresponds to the decrease in the amplitude of the off-transient that also occurs with high-frequency stimulation. 4. Another visual mutanttan, removes the off and on-transients of the ERG. 5. The combining of thestoned mutation withtan in thetan, stoned double mutant results in the loss of the jump behavior as well as the partial restoration of the off-transient to an otherwisetan-like ERG. The relationship between the increase in the amplitude of the off-transient instoned flies and the eliciting of the jump response is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00735278
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  • 2
    Electronic Resource
    Electronic Resource
    The regulation of phosphorylation of a specific protein in synaptosomal fractions fromDrosophila heads: The effects of light and two visual mutants (1983)
    Springer
    Cellular and molecular neurobiology 3 (1983), S. 127-141 
    Details
    ISSN: 1573-6830
    Keywords: cyclic adenosine monophosphate ; calmodulin ; phosphorylation ; visual mutants ; Drosophila
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Protein IV from synaptosomal fractions ofDrosophila heads is phosphorylatedin vitro by an endogenous cyclic adenosine monophosphate (cAMP)-dependent protein kinase. Thein vivo phosphorylation of this protein is affected by light. 2. Two visual mutants,tan andstoned, exhibit altered levels ofin vivo phosphorylation of protein IV. Thetan strain shows depressedin vivo levels of phosphorylation of protein IV, whereasstoned shows an increase in thein vivo level of phosphorylation of this same protein. 3. Protein D is phosphorylatedin vitro by an endogenous Ca2+/calmodulindependent protein kinase and has a molecular weight identical to that of protein IV. Thestoned mutant strain shows an increase in thein vivo level of phosphorylation of protein D. 4. The data presented here suggest that the phosphorylation of protein IV, and perhaps D, may play a role in the early processing of visual information in the fly.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00735277
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    Paper (German National Licenses)
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