ECHS1 interacts with STAT3 and negatively regulates STAT3 signaling
ECHS1 interacts with STAT3 and negatively regulates STAT3 signaling
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DOI:
10.1016/j.febslet.2013.02.005
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发表时间:
2013-03-18
期刊:
影响因子:
3.5
通讯作者:
Zhang, Wei-Na
中科院分区:
文献类型:
--
作者:
Chang, Yan;Wang, Shao-Xin;Zhang, Wei-Na
Signal transducer and activator of transcription 3 (STAT3) is a critical transcriptional factor in a variety of cellular processes, and is frequently over-activated in a range of human tumors. However, the processes that regulate STAT3 activation need to be further clarified. With a yeast two-hybrid screening, we identified enoyl-CoA hydratase short chain 1 (ECHS1) as a novel STAT3 binding protein. We further confirmed the interaction between STAT3 and ECHS1 by GST-pull down and coimmnunoprecipitation. Importantly, we found that ECHS1 specifically represses STAT3 activity and negatively regulates the expression of several target genes of STAT3 through inhibiting STAT3 phosphorylation. Therefore, our findings will provide new insights into the mechanism of STAT3 signaling regulation.Structured summary of protein interactions:STAT3 physically interacts with ECHS1 by pull down (View interaction)STAT3 physically interacts with ECHS1 by two hybrid (View Interaction: 1, 2)ECHS1 physically interacts with STAT3 by anti tag co immunoprecipitation (View Interaction: 1, 2)STAT3 physically interacts with ECHS1 by anti bait co immunoprecipitation (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.