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
