N-Glycosylation Regulates Fibroblast Growth Factor Receptor/EGL-15 Activity in Caenorhabditis elegans in Vivo*
N-Glycosylation Regulates Fibroblast Growth Factor Receptor/EGL-15 Activity in Caenorhabditis elegans in Vivo*
复制标题
N-糖基化调节秀丽隐杆线虫体内成纤维细胞生长因子受体/EGL-15 活性*
DOI:
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发表时间:
2009
影响因子:
4.8
通讯作者:
T. Kinnunen
中科院分区:
文献类型:
--
作者:
U. Polanska;L. Duchesne;Janet C. Harries;D. Fernig;T. Kinnunen
The regulation of cell function by fibroblast growth factors (FGFs) classically occurs through a dual receptor system of a tyrosine kinase receptor (FGFR) and a heparan sulfate proteoglycan co-receptor. Mutations in some consensus N-glycosylation sites in human FGFR result in skeletal disorders and craniosynostosis syndromes, and biophysical studies in vitro suggest that N-glycosylation of FGFR alters ligand and heparan sulfate binding properties. The evolutionarily conserved FGFR signaling system of Caenorhabditis elegans has been used to assess the role of N-glycosylation in the regulation of FGFR signaling in vivo. The C. elegans FGF receptor, EGL-15, is N-glycosylated in vivo, and genetic substitution of specific consensus N-glycosylation sites leads to defects in the maintenance of fluid homeostasis and differentiation of sex muscles, both of which are phenotypes previously associated with hyperactive EGL-15 signaling. These phenotypes are suppressed by hypoactive mutations in EGL-15 downstream signaling components or activating mutations in the phosphatidylinositol 3-kinase pathway, respectively. The results show that N-glycans negatively regulate FGFR activity in vivo supporting the notion that mutation of N-glycosylation sites in human FGFR may lead to inappropriate activation of the receptor.
影响因子:
2.7
作者:
Lo,Te-Wen;Branda,CatherineS;Huang,Peng;Sasson,IsaacE;Goodman,SJay;Stern,MichaelJ
通讯作者:
Stern,MichaelJ
影响因子:
9.8
作者:
White, KE;Cabral, JM;Econs, MJ
通讯作者:
Econs, MJ
影响因子:
11.4
作者:
MELLO, CC;KRAMER, JM;AMBROS, V
通讯作者:
AMBROS, V