Schlichter D, Miller H, Wicks W D
J Cyclic Nucleotide Protein Phosphor Res. 1986;11(3):149-54.
Transcriptional regulation by cAMP has been demonstrated for several eukaryotic genes; however, the identity of the protein kinase subunit involved has been a source of debate. Based on homologies with the procaryotic cAMP-binding catabolite activator protein, a recent hypothesis has invoked the regulatory protein RII as the mediator. The evidence currently available on the effects of microinjected kinase subunits suggests, however, that the catalytic subunit is the active factor. Moreover, the proposed homologies between the catabolite activator protein and RII are difficult to reconcile with its proposed mediatory role. We suggest as an alternative hypothesis that a phosphoprotein other than RII may mediate the effects of cAMP on eukaryotic gene expression.
环磷酸腺苷（cAMP）对几种真核基因的转录调控作用已得到证实；然而，所涉及的蛋白激酶亚基的身份一直是一个争论焦点。基于与原核cAMP结合分解代谢物激活蛋白的同源性，最近有一个假说认为调节蛋白RII是介导因子。然而，目前有关显微注射激酶亚基作用的现有证据表明，催化亚基才是活性因子。此外，分解代谢物激活蛋白与RII之间所提出的同源性难以与其所提出的介导作用相协调。我们提出另一种假说，即除RII之外的一种磷蛋白可能介导cAMP对真核基因表达的影响。
