IL-4 receptor α in non-lipid rafts is the target molecule of strictinin in inhibiting STAT6 activation

Biochem Biophys Res Commun. 2014 Jul 18;450(1):824-30. doi: 10.1016/j.bbrc.2014.06.069. Epub 2014 Jun 21.

Abstract

Strictinin has been shown to suppress interleukin (IL)-4-induced signal transducer and activator of transcription (STAT)-6 phosphorylation, which is a critical event for IgE class switching. However, it is unclear how strictinin inhibits STAT6 activation. Strictinin inhibited STAT6 phosphorylation by suppressing IL-4 receptor α (IL-4Rα) activation. Strictinin was bound to the cell surface and only localized in non-lipid raft fraction of the cells where IL-4Rα was also located. In addition, strictinin directly bound to IL-4Rα and inhibited binding of IL-4 to IL-4Rα. These results suggest that IL-4Rα locating in non-lipid raft region is a target molecule for strictinin in inhibiting STAT6 activation.

Keywords: IgE; Interleukin-4 receptor; Lipid rafts; Molecular target; Strictinin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Burkitt Lymphoma
  • HeLa Cells
  • Humans
  • Interleukin-4 / metabolism*
  • Membrane Microdomains / metabolism*
  • Mice
  • NIH 3T3 Cells
  • Phenols / pharmacology*
  • Phosphorylation / drug effects
  • Receptors, Interleukin-4 / antagonists & inhibitors*
  • Receptors, Interleukin-4 / metabolism*
  • STAT6 Transcription Factor / metabolism*
  • Transcriptional Activation / drug effects

Substances

  • IL4 protein, human
  • Phenols
  • Receptors, Interleukin-4
  • STAT6 Transcription Factor
  • STAT6 protein, human
  • strictinin
  • Interleukin-4