奶油
磷酸化
生物
福斯科林
丝氨酸
分子生物学
激酶
转录因子
蛋白激酶A
基因
细胞生物学
生物化学
体外
作者
Gustavo González,Marc Montminy
出处
期刊:Cell
[Elsevier]
日期:1989-11-01
卷期号:59 (4): 675-680
被引量:2486
标识
DOI:10.1016/0092-8674(89)90013-5
摘要
In this paper, we demonstrate that phosphorylation of CREB at Ser-133 is induced 6-fold in vivo, following treatment of PC12 cells with forskolin. By contrast, no such induction was observed in the kinase A-deficient PC12 line A126-1B2 (A126). Using F9 teratocarcinoma cells, which are unresponsive to cAMP, we initiated a series of transient expression experiments to establish a causal link between phosphorylation of CREB and trans-activation of cAMP-responsive genes. Inactivating the kinase A phosphorylation site by in vitro mutagenesis of the cloned CREB cDNA at Ser-133 completely abolished CREB transcriptional activity. As CREB mutants containing acidic residues in place of the Ser-133 phosphoacceptor were also transcriptionally inactive, these results suggest that phosphorylation of CREB may stimulate transcription by a mechanism other than by simply providing negative charge.
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