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FEBS Lett. 2011 Sep 2;585(17):2698-702. doi: 10.1016/j.febslet.2011.07.024. Epub 2011 Jul 26.

Investigating the mechanism of the assembly of FGF1-binding heparan sulfate motifs.

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1
Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA.

Abstract

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.

PMID:
21803043
PMCID:
PMC3163756
DOI:
10.1016/j.febslet.2011.07.024
[Indexed for MEDLINE]
Free PMC Article
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