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Novel recognition motif on fibroblast growth factor receptor mediates direct association and activation of SNT

H Xu1, K W Lee, M Goldfarb

  • 1Brookdale Center for Developmental and Molecular Biology, Cellular, Biochemical and Developmental Sciences, Mount Sinai School of Medicine, New York, New York 10029, USA.

The Journal of Biological Chemistry
|July 11, 1998
PubMed

Insights

Fibroblast growth factor (FGF) signaling involves adapter proteins SNT-1 and SNT-2, which directly link FGF receptor-1 to downstream pathways. This interaction is crucial for cellular signaling and is mediated by specific receptor and adapter protein domains.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • Fibroblast growth factors (FGFs) are key regulators of cellular processes.
  • FGF signaling pathways are initiated by FGF binding to FGF receptors (FGFRs).
  • Adapter proteins like FRS2/SNT-1 are involved in relaying signals downstream of FGFRs.

Purpose of the Study:

  • To investigate the direct interaction between FGF receptor-1 (FGFR-1) and adapter proteins SNT-1 and SNT-2.
  • To identify the specific domains within FGFR-1 and SNTs responsible for their interaction.
  • To elucidate the role of SNT proteins as direct links between FGFR-1 and downstream signaling pathways.

Main Methods:

  • Yeast two-hybrid protein-protein interaction assays were employed.
  • In vitro binding assays were conducted.
  • In vivo tyrosine phosphorylation of SNT proteins was analyzed.

Main Results:

  • Both SNT-1 and the newly identified SNT-2 protein directly bind to FGFR-1.
  • A juxtamembrane segment of FGFR-1 and the phosphotyrosine-binding domain of SNTs are essential and sufficient for this interaction.
  • FGFR-mediated tyrosine phosphorylation of SNTs in vivo requires these specific domains.
  • The SNT binding motif on FGFR-1 is unique, lacking tyrosine and asparagine residues typical of other phosphotyrosine-binding domain recognition motifs.

Conclusions:

  • SNT proteins (SNT-1 and SNT-2) act as direct molecular adaptors connecting FGFR-1 to downstream signaling cascades.
  • The identified interaction domains provide insights into the specificity of FGFR-1 signaling.
  • These findings expand the understanding of signal transduction mechanisms initiated by FGFs.

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