کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2047949 1074046 2011 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Investigating the mechanism of the assembly of FGF1-binding heparan sulfate motifs
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Investigating the mechanism of the assembly of FGF1-binding heparan sulfate motifs
چکیده انگلیسی

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.


► Combinatorial enzymatic modifications generate distinct heparan sulfate motifs.
► Concurrent enzymatic modification fails to produce FGF1-binding HS motifs.
► Sequentially modified HS structures form ternary complexes with FGF1/FGFR.
► GAGOSOMES may act in an orderly manner to generate divergent HS structures in vivo.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 585, Issue 17, 2 September 2011, Pages 2698–2702
نویسندگان
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