PIASy-mediated repression of the Ets-1 is independent of its sumoylation
PIASy-mediated repression of the Ets-1 is independent of its sumoylation
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DOI：
10.1016/j.bbrc.2006.05.065
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发表时间：
2006-07-14
影响因子：
3.1
通讯作者：
Fukami, K
中科院分区：
文献类型：
--
作者：
Nishida, T;Terashima, M;Fukami, K
转录因子Ets-1参与许多生理过程，包括血管生成、造血发育和肿瘤进展，并且其活性可以通过与其他蛋白质的相互作用和翻译后修饰（例如磷酸化）来调节。在这里，我们表明，Ets-1是SUMO修饰的目标，在体内和体外。突变分析表明，类小泛素化的Ets-1发生在两个赖氨酸残基的氨基酸位置15和227，位于先前确定的协同控制基序。用精氨酸替换SUMO化位点赖氨酸或过表达SENP 1（一种去SUMO化酶），可增强Ets-1的反式激活能力。此外，我们确定PIASy作为一种新的相互作用伙伴和Ets-1的特异性SUMO-E3连接酶。PIASy抑制Ets-1依赖的转录，并且其抑制不依赖于Ets-1的sumoylation状态，但依赖于其他因子的sumoylation。(c)2006年爱思唯尔公司All rights reserved.
The transcription factor Ets-1 is involved in many physiological processes, including angiogenesis, hematopoietic development, and tumor progression, and its activity can be regulated by interactions with other proteins and post-translational modifications, such as phosphorylation. Here, we show that Ets-1 is a target for SUMO modification both in vivo and in vitro. Mutational analysis reveals that sumoylation of Ets-1 occurs at two lysine residues at amino acid positions 15 and 227, which lie within previously identified synergy control motifs. Replacement of sumoylation site lysines with arginine or overexpression of SENP1, a desumoylation enzyme, enhances the transactivation ability of Ets-1. Furthermore, we identify PIASy as a novel interaction partner and a specific SUMO-E3 ligase of Ets-1. PIASy represses the Ets-1-dependent transcription, and its repression is independent of the sumoylation status of Ets-1, but it is dependent on the sumoylation of other factors. (c) 2006 Elsevier Inc. All rights reserved.