作者: T. Smeal , M. Hibi , M. Karin
DOI: 10.1002/J.1460-2075.1994.TB06946.X
关键词: Biology 、 MAP2K7 、 Protein kinase A 、 Protein phosphorylation 、 Autophagy-related protein 13 、 c-jun 、 Activating transcription factor 2 、 Cyclin-dependent kinase 2 、 Transactivation 、 Molecular biology
摘要: Protein phosphorylation is commonly used to modulate transcription factor activity. However, all existing genetic evidence for stimulation of activity by rests on loss-of-function mutations. To demonstrate conclusively that a potentiates its transactivation potential in vivo, we constructed c-Jun mutant phosphorylated the cAMP-sensitive protein kinase A (PKA) instead UV- and Ras-responsive JNK. The transcriptional this enhanced PKA, but not JNK activation. These results provide positive conclusive proof critical site (Ser73) located activation domain directly responsible enhancing function.