The FGFR D3 Domain Determines Receptor Selectivity For Fibroblast Growth Factor 21.

Gupte, J., Yang, L., Wu, X., Weiszmann, J., Hecht, R., Lemon, B., Lindberg, R., Wang, Z., Li, Y.
Journal   J Mol Biol.
Analytes Measured  
Matrix Tested   L6 cell lysates
Year   2011
Page Numbers  
Application   Phosphoproteins
FGF21 is a member of a unique subfamily of fibroblast growth factors that function as endocrine hormones and regulate a variety of metabolic activities. Unlike paracrine FGFs, FGF21 does not bind heparin and requires βKlotho as a co-receptor to activate FGFR signaling. In the presence of βKlotho, FGF21 is able to activate FGFRs 1c, 2c and 3c but not FGFR4. Chimeric FGFR1c/FGFR4 receptors were constructed to identify domains that confer this specificity and to understand regions important for FGF21-induced receptor activation. With these chimeras, we showed that domain 3 of the FGFR1c extracellular domain plays a critical role in specificity determination and receptor activation by FGF21. Furthermore, we were able to narrow down the sequences important for this function to a six amino acid region within domain 3 of FGFR1c. It is interesting to note that this region falls into the βC'-βE loop, which has been shown to be important for receptor specificity determination in paracrine FGFs, suggesting a common principle in both endocrine and paracrine FGF receptor interaction and activation.

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