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Updated: May 25, 2026

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
07:32

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

Published on: September 30, 2019

Molecular networks in FGF signaling: flotillin-1 and cbl-associated protein compete for the binding to fibroblast

Ana Tomasovic1, Stephanie Traub, Ritva Tikkanen

  • 1Institute of Biochemistry, University of Giessen, Giessen, Germany.

Plos One
|January 12, 2012
PubMed

Insights

Fibroblast growth factor receptor substrate 2 (FRS2α) interacts with novel proteins flotillin-1 and CAP. These interactions reveal a new signaling network crucial for receptor tyrosine kinase and MAPK pathway regulation.

Area of Science:

  • Cellular signaling
  • Molecular biology
  • Signal transduction

Background:

  • Fibroblast growth factor receptor substrate 2 (FRS2α) is a key signaling adaptor protein.
  • FRS2α regulates downstream signaling of receptor tyrosine kinases (RTKs).
  • FRS2α undergoes phosphorylation and forms complexes with other signaling molecules.

Purpose of the Study:

  • To identify novel interaction partners of FRS2α.
  • To elucidate the role of these interactions in RTK signaling.
  • To characterize the FRS2α, flotillin-1, and CAP signaling network.

Main Methods:

  • Co-immunoprecipitation assays to identify protein interactions.
  • Western blotting to assess protein phosphorylation.
  • RNA interference (siRNA) to knockdown flotillin-1 expression.

Main Results:

  • Flotillin-1 and cbl-associated protein/ponsin (CAP) were identified as novel FRS2α interaction partners.
  • Flotillin-1 binds to the PTB domain of FRS2α, competing with FGFR binding and increasing FRS2α phosphorylation.
  • CAP interacts with FRS2α via its SoHo domain and SH3 domain, suggesting competition with flotillin-1 for FRS2α binding.

Conclusions:

  • A novel signaling network involving FRS2α, flotillin-1, and CAP has been identified.
  • The successive interactions within this network are critical for regulating RTK signaling.
  • This network plays a significant role in modulating the mitogen-activated protein kinase (MAPK) pathway.

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