Intermolecular relations between the glucocorticoid receptor, ZAP-70 kinase, and Hsp-90

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Abstract

The glucocorticoid receptor (GR) participates in both genomic and non-genomic glucocorticoid hormone (GC) actions by interacting with other cytoplasmic signalling proteins. Previously, we have shown that high dose Dexamethasone (DX) treatment of Jurkat cells causes tyrosine phosphorylation of ZAP-70 within 5 min in a GR-dependent manner. By using co-immunoprecipitation and confocal microscopy, here we demonstrate that the liganded GR physically associates with ZAP-70, in addition to its phosphorylation changes. The association of the ligand-bound GR and ZAP-70 was also observed in HeLa cells transfected with ZAP-70, suggesting that this co-clustering is independent of lymphocyte specific factors. Furthermore, the ZAP-70 was found to also co-precipitate with Hsp-90 chaperone both in Jurkat and transgenic HeLa cells, independent of the presence of DX. These findings raise the possibility that ZAP-70 may serve as an important link between GC and TcR-induced signaling, thereby transmitting non-genomic GC action in T-cells.

Original languageEnglish
Pages (from-to)253-258
Number of pages6
JournalBiochemical and biophysical research communications
Volume354
Issue number1
DOIs
Publication statusPublished - Mar 2 2007

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Keywords

  • Glucocorticoid receptor (GR)
  • Hsp-90
  • Jurkat cells
  • Non-genomic glucocorticoid effects
  • ZAP-70

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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