EGF induces nuclear translocation of STAT2 without tyrosine phosphorylation in intestinal epithelial cells

Leonard R. Johnson, Shirley A. McCormack, Chuan Yang, Susan R. Pfeffer, Lawrence Pfeffer

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Signal transducers and activators of transcription (STATs) are cytoplasmic proteins that bind to activated membrane receptors, undergo ligand-dependent phosphorylation on tyrosine residues, and translocate to the nucleus, where they induce transcription of specific genes in response to a variety of ligands, including cytokines and some growth factors. Using immunocytochemical and biochemical techniques, we investigated the localization and responses of STAT1 and STAT2 to epidermal growth factor (EGF) stimulation in IEC-6 intestinal epithelial cells and HeLa cells. These studies provide the first description of STAT activation and localization in response to EGF in intestinal epithelial cells and some novel findings regarding the activation and localization of STATs in general. These include the following. First, EGF promoted the tyrosine phosphorylation of STAT1 in IEC-6 cells and caused its translocation to the nucleus. Second, in the absence of EGF stimulation both STAT1 and STAT2 were localized to the Golgi apparatus in IEC-6 cells. Third, EGF caused the translocation of STAT2 to the nucleus in both IEC-6 and HeLa cells without inducing the tyrosine phosphorylation of STAT2.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Cell Physiology
Volume276
Issue number2 45-2
StatePublished - Mar 5 1999

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Epidermal Growth Factor
Tyrosine
Epithelial Cells
Phosphorylation
Transducers
HeLa Cells
STAT Transcription Factors
Ligands
Golgi Apparatus
Transcriptional Activation
Intercellular Signaling Peptides and Proteins
Cytokines
Membranes
Genes

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cell Biology

Cite this

EGF induces nuclear translocation of STAT2 without tyrosine phosphorylation in intestinal epithelial cells. / Johnson, Leonard R.; McCormack, Shirley A.; Yang, Chuan; Pfeffer, Susan R.; Pfeffer, Lawrence.

In: American Journal of Physiology - Cell Physiology, Vol. 276, No. 2 45-2, 05.03.1999.

Research output: Contribution to journalArticle

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AB - Signal transducers and activators of transcription (STATs) are cytoplasmic proteins that bind to activated membrane receptors, undergo ligand-dependent phosphorylation on tyrosine residues, and translocate to the nucleus, where they induce transcription of specific genes in response to a variety of ligands, including cytokines and some growth factors. Using immunocytochemical and biochemical techniques, we investigated the localization and responses of STAT1 and STAT2 to epidermal growth factor (EGF) stimulation in IEC-6 intestinal epithelial cells and HeLa cells. These studies provide the first description of STAT activation and localization in response to EGF in intestinal epithelial cells and some novel findings regarding the activation and localization of STATs in general. These include the following. First, EGF promoted the tyrosine phosphorylation of STAT1 in IEC-6 cells and caused its translocation to the nucleus. Second, in the absence of EGF stimulation both STAT1 and STAT2 were localized to the Golgi apparatus in IEC-6 cells. Third, EGF caused the translocation of STAT2 to the nucleus in both IEC-6 and HeLa cells without inducing the tyrosine phosphorylation of STAT2.

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