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Interaction of fibroblast growth factor receptor 3 and the adapter protein SH2-B. A role in STAT5 activation

Monica Kong1, Ching S Wang, Daniel J Donoghue

  • 1Department of Chemistry and Biochemistry, Center for Molecular Genetics, University of California San Diego, La Jolla, California 92093-0367, USA.

The Journal of Biological Chemistry
|February 6, 2002
PubMed

Insights

Fibroblast growth factor receptor 3 (FGFR3) interacts with SH2-B beta, a novel adapter protein. This interaction mediates FGFR3 signaling, impacting cell growth and cancer development.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Cancer Research

Background:

  • Fibroblast growth factor receptor 3 (FGFR3) is crucial for cell growth, differentiation, and migration.
  • Activating mutations in FGFR3 are linked to various cancers, including multiple myeloma and bladder cancer.

Purpose of the Study:

  • To identify proteins interacting with FGFR3 that may mediate its signaling pathways.
  • To elucidate the role of SH2-B beta in FGFR3-dependent signal transduction.

Main Methods:

  • Yeast two-hybrid screen using the FGFR3 kinase domain.
  • Coimmunoprecipitation assays in 293T cells.
  • Analysis of tyrosine phosphorylation sites and Stat5 activation.

Main Results:

  • SH2-B beta was identified as an FGFR3-interacting protein.
  • FGFR3 activation leads to tyrosine phosphorylation of SH2-B beta, dependent on specific FGFR3 tyrosine residues (Tyr-724 and Tyr-760).
  • Activated FGFR3 phosphorylates and translocates Stat5, with increased Stat5 activity upon SH2-B beta overexpression.

Conclusions:

  • SH2-B beta is a novel binding partner for FGFR3.
  • SH2-B beta mediates FGFR3 signal transduction, influencing Stat5 activation.

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