Related Experiment Video

Updated: Aug 7, 2026

Reprogramming Mouse Embryonic Fibroblasts with Transcription Factors to Induce a Hemogenic Program
11:00

Reprogramming Mouse Embryonic Fibroblasts with Transcription Factors to Induce a Hemogenic Program

Published on: December 16, 2016

Reprogramming FGFR isoform specificity in FGF2 by deep mutational scanning

Yuga Okada1, Jumpei Morimoto1, Shinsuke Sando1,2

  • 1Department of Chemistry and Biotechnology, The University of Tokyo 7-3-1 Hongo Bunkyo-ku Tokyo 113-8656 Japan ssando@chembio.t.u-tokyo.ac.jp.

Chemical Science
|August 6, 2026
PubMed

Insights

Researchers engineered fibroblast growth factor 2 (FGF2) variants with altered fibroblast growth factor receptor (FGFR) specificity. Single-amino acid changes successfully reprogrammed receptor selectivity, enabling tailored FGF/FGFR signaling network control.

Area of Science:

  • Molecular biology
  • Biochemistry
  • Signaling pathways

Background:

  • The fibroblast growth factor (FGF) family and its seven fibroblast growth factor receptor (FGFR) isoforms form complex signaling networks.
  • FGF2 has significant physiological roles and therapeutic potential, but its broad FGFR activation causes adverse effects.
  • Engineering FGF ligands for controlled FGFR isoform specificity is crucial for therapeutic applications.

Purpose of the Study:

  • To engineer FGF2 variants with altered FGFR isoform specificity.
  • To identify key residues in the FGFR-binding interface that determine receptor specificity.
  • To establish a framework for designing FGF ligands with tailored specificity.

Main Methods:

  • Utilized mRNA display-based deep mutational scanning (DMS) to engineer FGF2 variants.
  • Systematically evaluated residues within the FGFR-binding interface.
  • Assessed the FGFR isoform specificity of engineered FGF2 variants.

Main Results:

  • Successfully generated FGF2 variants with altered FGFR isoform specificity.
  • Demonstrated that FGFR isoform specificity is malleable and can be reprogrammed.
  • Identified single-amino acid substitutions as sufficient to alter receptor selectivity.

Conclusions:

  • Receptor selectivity in FGF2 is tunable.
  • Provided a method for rationally designing FGF ligands with specific FGFR isoform targeting.
  • Advanced the understanding and control of FGF/FGFR signaling networks.

More Related Videos

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library07:32

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

Published on: September 30, 2019

HOX Loci Focused CRISPR/sgRNA Library Screening Identifying Critical CTCF Boundaries10:10

HOX Loci Focused CRISPR/sgRNA Library Screening Identifying Critical CTCF Boundaries

Published on: March 31, 2019

Related Concept Videos

Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...