Source:http://linkedlifedata.com/resource/pubmed/id/10199968
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1999-5-17
|
| pubmed:abstractText |
Formin was originally isolated as the gene affected by the murine limb deformity (ld) mutations, which disrupt the epithelial-mesenchymal interactions regulating patterning of the vertebrate limb autopod. More recently, a rapidly growing number of genes with similarity to formin have been isolated from many different species including fungi and plants. Genetic and biochemical analysis shows that formin family members function in cellular processes regulating either cytokinesis and/or cell polarisation. Another common feature among formin family members is their requirement in morphogenetic processes such as budding and conjugation of yeast, establishment of Drosophila oocyte polarity and vertebrate limb pattern formation. Vertebrate formins are predominantly nuclear proteins which control polarising activity in limb buds through establishment of the SHH/FGF-4 feedback loop. Formin acts in the limb bud mesenchyme to induce apical ectodermal ridge (AER) differentiation and FGF-4 expression in the posterior AER compartment. Finally, disruption of the epithelial-mesenchymal interactions controlling induction of metanephric kidneys in ld mutant embryos indicates that formin might function more generally in transduction of morphogenetic signals during embryonic pattern formation.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fetal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/formin 1
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0302-766X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
296
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
85-93
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10199968-Amino Acid Sequence,
pubmed-meshheading:10199968-Animals,
pubmed-meshheading:10199968-Body Patterning,
pubmed-meshheading:10199968-Evolution, Molecular,
pubmed-meshheading:10199968-Extremities,
pubmed-meshheading:10199968-Fetal Proteins,
pubmed-meshheading:10199968-Humans,
pubmed-meshheading:10199968-Limb Deformities, Congenital,
pubmed-meshheading:10199968-Mice,
pubmed-meshheading:10199968-Microfilament Proteins,
pubmed-meshheading:10199968-Molecular Sequence Data,
pubmed-meshheading:10199968-Morphogenesis,
pubmed-meshheading:10199968-Multigene Family,
pubmed-meshheading:10199968-Nuclear Proteins,
pubmed-meshheading:10199968-Phylogeny,
pubmed-meshheading:10199968-Sequence Alignment,
pubmed-meshheading:10199968-Sequence Homology, Amino Acid,
pubmed-meshheading:10199968-Signal Transduction,
pubmed-meshheading:10199968-Transcription Factors
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| pubmed:year |
1999
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| pubmed:articleTitle |
Formin defines a large family of morphoregulatory genes and functions in establishment of the polarising region.
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| pubmed:affiliation |
European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany. r.zeller@bio.uu.nl
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| pubmed:publicationType |
Journal Article,
Review
|