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Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis
10:22

Protein Purification-free Method of Binding Affinity Determination by Microscale Thermophoresis

Published on: August 15, 2013

Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein

C L Yu1, D J Meyer, G S Campbell

  • 1Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor 48109, USA.

Science (New York, N.Y.)
|July 7, 1995
PubMed

Insights

The Src oncogene activates signal transducers and activators of transcription (STATs), specifically Stat3. This constitutive activation of STAT signaling by Src may contribute to cancer development.

Area of Science:

  • Molecular Biology
  • Oncology
  • Cell Signaling

Background:

  • Signal transducers and activators of transcription (STATs) are key mediators of gene expression.
  • Cytokines and growth factors typically induce STAT tyrosine phosphorylation and activation.

Purpose of the Study:

  • To investigate STAT protein activation in cells transformed by the Src oncogene tyrosine kinase.
  • To determine if Src oncoprotein can constitutively activate STAT signaling pathways.

Main Methods:

  • Electrophoretic mobility assays
  • DNA-binding specificity assays
  • Antigenicity assays
  • Analysis of tyrosine phosphorylation of Stat3

Main Results:

  • Stat3 or a related STAT family member was constitutively activated in Src-transformed cells.
  • This activation involved tyrosine phosphorylation of Stat3.
  • The induced DNA-binding activity correlated with Src-mediated transformation.

Conclusions:

  • Src oncoprotein can activate STAT signaling pathways.
  • Stat3 activation by Src suggests a potential role for Stat3 in Src-induced oncogenesis.

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