Nuclear protein NP60 regulates p38 MAPK activity
Nuclear protein NP60 regulates p38 MAPK activity
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DOI：
10.1242/jcs.02699
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发表时间：
2006-01-01
影响因子：
4
通讯作者：
Gu, J
中科院分区：
文献类型：
--
作者：
Fu, J;Yang, ZQ;Gu, J
p38 α的激活由其上游激酶和相关蛋白介导。在这里，我们确定了一个新的核蛋白，NP60，调节p38 α的激活响应山梨醇处理。在体外和体内，NP 60特异性结合p38 α，但不结合JNK和ERK。NP60的共转染导致p38 α的磷酸化和活化，并随后导致活化转录因子2的磷酸化和活化。由NP60诱导的p38 α的磷酸化需要p38 α MAP激酶、MAP激酶激酶6（MKK6）或MKK4的上游活性。我们的研究结果表明，NP60介导p38 α的应激激活，并以特定的方式调节p38 α信号。
The activation of p38 alpha is mediated by its upstream kinase and associated proteins. Here we identify a new nuclear protein, NP60, which regulates the activation of p38 alpha in response to sorbitol treatment. NP60 specifically binds to p38 alpha, but not to JNK and ERK, in vitro and in vivo. Cotransfection of NP60 leads to the phosphorylation and activation of p38 alpha, and subsequently results in the phosphorylation and activation of activating transcription factor 2. The phosphorylation of p38 alpha induced by NP60 requires upstream activity of p38 alpha MAP kinase, MAP kinase kinase 6 (MKK6) or MKK4. Our results indicate that NP60 mediates stress activation of p38 alpha and regulates p38 alpha signaling in a specific way.