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Investigating the mechanism of the assembly of FGF1‐binding heparan sulfate motifs
Author(s) -
Nu Nguyen Thao Kim,
Raman Karthik,
Tran Vy My,
Kuberan Balagurunathan
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.07.024
Subject(s) - heparan sulfate , fgf1 , mechanism (biology) , chemistry , microbiology and biotechnology , biophysics , biochemistry , fibroblast growth factor , biology , fibroblast growth factor receptor , glycosaminoglycan , receptor , philosophy , epistemology
Heparan sulfate (HS) chains play crucial biological roles by binding to various signaling molecules including fibroblast growth factors (FGFs). Distinct sulfation patterns of HS chains are required for their binding to FGFs/FGF receptors (FGFRs). These sulfation patterns are putatively regulated by biosynthetic enzyme complexes, called GAGOSOMES, in the Golgi. While the structural requirements of HS–FGF interactions have been described previously, it is still unclear how the FGF‐binding motif is assembled in vivo. In this study, we generated HS structures using biosynthetic enzymes in a sequential or concurrent manner to elucidate the potential mechanism by which the FGF1‐binding HS motif is assembled. Our results indicate that the HS chains form ternary complexes with FGF1/FGFR when enzymes carry out modifications in a specific manner.