Kelly L E
Cell Mol Neurobiol. 1983 Jun;3(2):127-41. doi: 10.1007/BF00735277.
Protein IV from synaptosomal fractions of Drosophila heads is phosphorylated in vitro by an endogenous cyclic adenosine monophosphate (cAMP)-dependent protein kinase. The in vivo phosphorylation of this protein is affected by light. Two visual mutants, tan and stoned, exhibit altered levels of in vivo phosphorylation of protein IV. The tan strain shows depressed in vivo levels of phosphorylation of protein IV, whereas stoned shows an increase in the in vivo level of phosphorylation of this same protein. Protein D is phosphorylated in vitro by an endogenous Ca2+/calmodulin-dependent protein kinase and has a molecular weight identical to that of protein IV. The stoned mutant strain shows an increase in the in vivo level of phosphorylation of protein D. 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.
果蝇头部突触体组分中的蛋白质IV在体外被内源性环磷酸腺苷（cAMP）依赖性蛋白激酶磷酸化。该蛋白质的体内磷酸化受光的影响。两种视觉突变体，棕褐色和麻木，表现出蛋白质IV体内磷酸化水平的改变。棕褐色品系显示蛋白质IV体内磷酸化水平降低，而麻木则显示该相同蛋白质体内磷酸化水平增加。蛋白质D在体外被内源性Ca2+/钙调蛋白依赖性蛋白激酶磷酸化，并且分子量与蛋白质IV相同。麻木突变品系显示蛋白质D体内磷酸化水平增加。此处呈现的数据表明，蛋白质IV以及可能的蛋白质D的磷酸化可能在果蝇视觉信息的早期处理中起作用。
