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Extracellular interactome of the FGF receptor–ligand system: Complexities and the relative simplicity of the worm
Author(s) -
Polanska Urszula M.,
Fernig David G.,
Kinnunen Tarja
Publication year - 2009
Publication title -
developmental dynamics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.634
H-Index - 141
eISSN - 1097-0177
pISSN - 1058-8388
DOI - 10.1002/dvdy.21757
Subject(s) - biology , fibroblast growth factor receptor , fibroblast growth factor , microbiology and biotechnology , alternative splicing , receptor , heparan sulfate , integrin , cell adhesion , signal transduction , gene isoform , genetics , cell , gene
Fibroblast growth factors (FGFs) and their receptors (FGFRs) regulate a multitude of biological functions in embryonic development and in adult. A major question is how does one family of growth factors and their receptors control such a variety of functions? Classically, specificity was thought to be imparted by alternative splicing of the FGFRs, resulting in isoforms that bind specifically to a subset of the FGFs, and by different saccharide sequences in the heparan sulfate proteoglycan (HSPG) co‐receptor. A growing number of noncanonical co‐receptors such as integrins and neural cell adhesion molecule (NCAM) are now recognized as imparting additional complexity to classic FGFR signaling. This review will discuss the noncanonical FGFR ligands and speculate on the possibility that they provide additional and alternative means to determining the functional specificity of FGFR signaling. We will also discuss how invertebrate models such as C. elegans may advance our understanding of noncanonical FGFR signaling. Developmental Dynamics 238:277–293, 2009. © 2008 Wiley‐Liss, Inc.