Wen Z, Zhong Z, Darnell J E
Laboratory of Molecular Cell Biology, Rockefeller University, New York, New York 10021-6399, USA.
Cell. 1995 Jul 28;82(2):241-50. doi: 10.1016/0092-8674(95)90311-9.
Stat1 and Stat3 are latent transcriptional factors activated initially through phosphorylation on single tyrosine residues induced by cytokine and growth factor occupation of cell surface receptors. Here we show that phosphorylation on a single serine (residue 727) in each protein is also required for maximal transcriptional activity. Both cytokines and growth factors are capable of inducing the serine phosphorylation of Stat1 and Stat3. These experiments show that gene activation by Stat1 and Stat3, which obligatorily require tyrosine phosphorylation to become active, also depends for maximal activation on one or more of the many serine kinases.
Stat1和Stat3是潜在的转录因子，最初通过细胞因子和生长因子占据细胞表面受体诱导的单个酪氨酸残基磷酸化而被激活。我们在此表明，每种蛋白质中单个丝氨酸（第727位残基）的磷酸化对于最大转录活性也是必需的。细胞因子和生长因子都能够诱导Stat1和Stat3的丝氨酸磷酸化。这些实验表明，Stat1和Stat3激活基因（它们必须通过酪氨酸磷酸化才能激活），其最大激活也依赖于众多丝氨酸激酶中的一种或多种。
