PHOSPHORYLATION OF C-JUN MEDIATED BY MAP KINASES
PHOSPHORYLATION OF C-JUN MEDIATED BY MAP KINASES
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DOI：
10.1038/353670a0
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发表时间：
1991-10-17
期刊：
影响因子：
64.8
通讯作者：
WOODGETT, JR
中科院分区：
文献类型：
--
作者：
PULVERER, BJ;KYRIAKIS, JM;WOODGETT, JR
原癌基因c-jun是AP-1转录因子家族的一个组成部分，参与细胞外刺激1-3引起的核事件的介导。c-jun蛋白通过羧基末端附近的残基的磷酸化负调节，所述残基响应于佛波醇酯而被去磷酸化4。在此，我们鉴定了氨基末端A1反式激活结构域中的两个丝氨酸残基，它们响应于多种有丝分裂原、佛波酯和激活的ras而被磷酸化（参考文献5）。我们目前的证据表明，促分裂原活化蛋白丝氨酸（MAP）激酶（pp 54和pp 42/44）特异性磷酸化这些网站，他们的磷酸化正调控c-jun的transacting activity。MAP激酶pp 54和pp 42/44的酪氨酸以及丝氨酸/苏氨酸磷酸化调节6，7。 MAP激酶激活c-jun可能是有丝分裂原、生长因子和癌基因共同刺激该转录因子的基础。
THE proto-oncogene c-jun is a component of the AP-1 transcription factor family involved in the mediation of nuclear events elicited by extracellular stimuli 1-3. The c-jun protein is negatively regulated by phosphorylation of residues near the carboxy terminus which are dephosphorylated in response to phorbol esters 4. Here we identify two serine residues in the amino terminal A1 transactivation domain which are phosphorylated in response to a variety of mitogens, phorbol esters and activated ras (ref. 5). We present evidence that mitogen-activated protein-serine (MAP) kinases (pp54 and pp42/44) specifically phosphorylate these sites and that their phosphorylation positively regulates the transacting activity of c-jun. The MAP kinase enzymes pp54 and pp42/44 are regulated by tyrosine as well as serine/threonine phosphorylation 6,7. MAP kinase activation of c-jun may underlie the common stimulation of this transcription factor by mitogens, growth factors and oncogenes.