Dévay P, Pintér M, Yalcin A S, Friedrich P
Neuroscience. 1986 May;18(1):193-203. doi: 10.1016/0306-4522(86)90188-0.
The phosphorylation-dephosphorylation, in the presence of adenosine 5'-[gamma-32P]triphosphate, of a polypeptide of apparent molecular mass 53,000 has been compared in head homogenates of wild type and memory mutant dunceM11 strains of Drosophila melanogaster. In both strains, labelling of the 53 kilodalton protein required exogenous adenosine 3',5'-phosphate (cAMP), but in dunceM11 cAMP at higher concentration (above approximately 3 microM) caused the rapid disappearance of the label. This differential dephosphorylation can be attributed to the lack of a cAMP-specific phosphodiesterase isoenzyme in the mutant. Several lines of evidence indicate that the 53 kilodalton protein is identical with the regulatory subunit of cAMP-dependent protein kinase. The findings suggest that in the mutant's nerve cells the state of phosphorylation of the regulatory subunit of cAMP-dependent protein kinase is altered, which may contribute to the biochemical disorder leading to the memory deficit.
在存在腺苷5'-[γ-32P]三磷酸的情况下，对野生型和记忆突变体果蝇黑腹果蝇dunceM11品系头部匀浆中表观分子量为53,000的多肽的磷酸化-去磷酸化进行了比较。在这两个品系中，53千道尔顿蛋白的标记需要外源性腺苷3',5'-磷酸（cAMP），但在dunceM11中，较高浓度（约3 microM以上）的cAMP会导致标记迅速消失。这种差异去磷酸化可归因于突变体中缺乏cAMP特异性磷酸二酯酶同工酶。几条证据表明，53千道尔顿蛋白与cAMP依赖性蛋白激酶的调节亚基相同。这些发现表明，在突变体的神经细胞中，cAMP依赖性蛋白激酶调节亚基的磷酸化状态发生了改变，这可能导致导致记忆缺陷的生化紊乱。
