ECHS1 interacts with STAT3 and negatively regulates STAT3 signaling

FEBS Lett. 2013 Mar 18;587(6):607-13. doi: 10.1016/j.febslet.2013.02.005. Epub 2013 Feb 14.

Abstract

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 co-immnunoprecipitation. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enoyl-CoA Hydratase / genetics*
  • Enoyl-CoA Hydratase / metabolism
  • Epidermal Growth Factor / pharmacology
  • Gene Expression Regulation, Neoplastic* / drug effects
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Immunoprecipitation
  • Interleukin-6 / pharmacology
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Phosphorylation
  • Protein Binding
  • STAT3 Transcription Factor / genetics*
  • STAT3 Transcription Factor / metabolism
  • Signal Transduction / drug effects
  • Two-Hybrid System Techniques

Substances

  • IL6 protein, human
  • Interleukin-6
  • Isoenzymes
  • STAT3 Transcription Factor
  • STAT3 protein, human
  • Epidermal Growth Factor
  • Enoyl-CoA Hydratase