Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-12-30
pubmed:abstractText
Fibroblast growth factor (FGF) signaling is necessary for both proliferation and differentiation of lens cells. However, the molecular mechanisms by which FGFs exert their effects on the lens remain poorly understood. In this study, we show that FGF-2 repressed the expression of lens-specific genes at the proliferative phase in primary cultured lens cells. Using transfected cells, we also found that the activity of L-Maf, a lens differentiation factor, is repressed by FGF/ERK signaling. L-Maf is shown to be phosphorylated by ERK, and introduction of mutations into the ERK target sites on L-Maf promotes its stabilization. The stable L-Maf mutant protein promotes the differentiation of lens cells from neural retina cells. Taken together, these results indicate that FGF/ERK signaling negatively regulates the function of L-Maf in proliferative lens cells and that stabilization of the L-Maf protein is important for lens fiber differentiation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 2, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Threonine, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/delta-Crystallins
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
537-44
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12393904-Animals, pubmed-meshheading:12393904-Cell Differentiation, pubmed-meshheading:12393904-Cells, Cultured, pubmed-meshheading:12393904-Chick Embryo, pubmed-meshheading:12393904-Cysteine Endopeptidases, pubmed-meshheading:12393904-Epithelial Cells, pubmed-meshheading:12393904-Eye Proteins, pubmed-meshheading:12393904-Fibroblast Growth Factor 2, pubmed-meshheading:12393904-Gene Expression Regulation, Developmental, pubmed-meshheading:12393904-Genes, Reporter, pubmed-meshheading:12393904-Humans, pubmed-meshheading:12393904-Immunohistochemistry, pubmed-meshheading:12393904-Lens, Crystalline, pubmed-meshheading:12393904-MAP Kinase Signaling System, pubmed-meshheading:12393904-Mitogen-Activated Protein Kinases, pubmed-meshheading:12393904-Multienzyme Complexes, pubmed-meshheading:12393904-Phosphorylation, pubmed-meshheading:12393904-Proteasome Endopeptidase Complex, pubmed-meshheading:12393904-Recombinant Fusion Proteins, pubmed-meshheading:12393904-Serine, pubmed-meshheading:12393904-Threonine, pubmed-meshheading:12393904-Transcription Factors, pubmed-meshheading:12393904-delta-Crystallins
pubmed:year
2003
pubmed:articleTitle
The stability of the lens-specific Maf protein is regulated by fibroblast growth factor (FGF)/ERK signaling in lens fiber differentiation.
pubmed:affiliation
Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma 630-0101, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't