Functional regulation of TEL by p38-induced phosphorylation
Functional regulation of TEL by p38-induced phosphorylation
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DOI：
10.1016/s0006-291x(02)02588-3
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发表时间：
2002-11-22
影响因子：
3.1
通讯作者：
Mitani, K
中科院分区：
文献类型：
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作者：
Arai, H;Maki, K;Mitani, K
TEL是属于ETS家族转录因子的核磷蛋白。TEL作为一种肿瘤抑制因子，对新生儿骨髓造血的建立至关重要。由于TEL具有多个假定的促分裂原活化蛋白（MAP）激酶磷酸化位点，我们在这里研究了通过应激信号通路对TEL的功能调节。我们发现，TEL在体内被激活的p38磷酸化，而不是JNK1。组成型和诱导型磷酸化位点分别为Ser（22）和Ser（257）。TEL与p38结合并在体外被p38直接磷酸化。体内p38依赖性磷酸化通过ETS结合共有位点降低TEL的反式抑制能力。这些数据表明，TEL的功能可能受到p38的调节，p38被各种应激激活。TEL可能是信号转导系统中特异性MAP激酶的下游成分。(C)2002 Elsevier Science（美国）。All rights reserved.
TEL is a nuclear phosphoprotein that belongs to a member of the ETS family transcription factors. TEL acts as a tumor suppressor and is essential for establishing hematopoiesis in neonatal bone marrow. Because TEL possesses multiple putative mitogen-activated protein (MAP) kinase phosphorylation sites, we here investigated functional regulation of TEL via stress signaling pathways. We showed that TEL becomes phosphorylated in vivo by activated p38 but not by JNK1. The constitutive and inducible phosphorylation sites were found to be Ser(22) and Ser(257), respectively. TEL bound to p38 and was directly phosphorylated in vitro by p38. In vivo p38-dependent phosphorylation reduced trans-repressional abilities of TEL through ETS-binding consensus site. These data indicate that TEL's functions are potentially regulated by p38 which is activated by various kinds of stresses. TEL could be a constituent downstream of the specific MAP kinase in the signal transduction system. (C) 2002 Elsevier Science (USA). All rights reserved.