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The FGFR D3 domain determines receptor selectivity for fibroblast growth factor 21.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Gupte J,Yang L,Wu X,Weiszmann J,Hecht R,Lemon B,Lindberg R,Wang Z,Li Y

doi

10.1016/j.jmb.2011.03.003

subject

Has Abstract

pub_date

2011-05-06 00:00:00

pages

491-502

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(11)00255-5

journal_volume

408

pub_type

杂志文章

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