Supplementary Figure S5 from The C-Terminal Kinase Domain–Binding and Suppression Motif Prevents Constitutive Activation of FGFR2

Key Points

FACS data reveal fgfr2 internalization patterns that prevent unwanted activation.
The analysis demonstrates that the c-terminal motif plays a critical role in kinase domain interactions.
Assessment using biochemical fgfr2-CT assays supports findings about suppressive effects on fgfr2 activity.
This work highlights the importance of the kinase binding motif and its implications for fgfr2 regulation.

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FACS data shows fgfr2 internalization in assays, suggesting kinase domain motif's role in preventing activation.

FACS data incl. gating strategy supporting the HALO Fgfr2 internalization analysis and data supporting the biochemical Fgfr2-CT assays

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Zingg et al. (2025) studied this question.

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