自磷酸化
p38丝裂原活化蛋白激酶
茴香霉素
丝裂原活化蛋白激酶
激酶
磷酸化
细胞生物学
化学
蛋白激酶A
生物
MAPK/ERK通路
生物化学
作者
Baoxue Ge,Hermann Gram,Franco Di Padova,Betty Huang,Liguo New,Richard J. Ulevitch,Ying Luo,Jiahuai Han
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2002-02-15
卷期号:295 (5558): 1291-1294
被引量:491
标识
DOI:10.1126/science.1067289
摘要
Phosphorylation of mitogen-activated protein kinases (MAPKs) on specific tyrosine and threonine sites by MAP kinase kinases (MAPKKs) is thought to be the sole activation mechanism. Here, we report an unexpected activation mechanism for p38alpha MAPK that does not involve the prototypic kinase cascade. Rather it depends on interaction of p38alpha with TAB1 [transforming growth factor-beta-activated protein kinase 1 (TAK1)-binding protein 1] leading to autophosphorylation and activation of p38alpha. We detected formation of a TRAF6-TAB1-p38alpha complex and showed stimulus-specific TAB1-dependent and TAB1-independent p38alpha activation. These findings suggest that alternative activation pathways contribute to the biological responses of p38alpha to various stimuli.
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