Source:http://linkedlifedata.com/resource/pubmed/id/19801543
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
48
|
| pubmed:dateCreated |
2009-11-25
|
| pubmed:abstractText |
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.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
1083-351X
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| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:day |
27
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| pubmed:volume |
284
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
33030-9
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| pubmed:dateRevised |
2011-3-3
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| pubmed:meshHeading |
pubmed-meshheading:19801543-Amino Acid Sequence,
pubmed-meshheading:19801543-Animals,
pubmed-meshheading:19801543-Animals, Genetically Modified,
pubmed-meshheading:19801543-Binding Sites,
pubmed-meshheading:19801543-Caenorhabditis elegans,
pubmed-meshheading:19801543-Caenorhabditis elegans Proteins,
pubmed-meshheading:19801543-Cell Differentiation,
pubmed-meshheading:19801543-Female,
pubmed-meshheading:19801543-Glycosylation,
pubmed-meshheading:19801543-Humans,
pubmed-meshheading:19801543-Male,
pubmed-meshheading:19801543-Microscopy, Fluorescence,
pubmed-meshheading:19801543-Molecular Sequence Data,
pubmed-meshheading:19801543-Muscle, Smooth,
pubmed-meshheading:19801543-Mutagenesis, Site-Directed,
pubmed-meshheading:19801543-Mutation,
pubmed-meshheading:19801543-Myoblasts,
pubmed-meshheading:19801543-Receptors, Fibroblast Growth Factor,
pubmed-meshheading:19801543-Sequence Homology, Amino Acid,
pubmed-meshheading:19801543-Signal Transduction
|
| pubmed:year |
2009
|
| pubmed:articleTitle |
N-Glycosylation regulates fibroblast growth factor receptor/EGL-15 activity in Caenorhabditis elegans in vivo.
|
| pubmed:affiliation |
School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, United Kingdom.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|