| pubmed-article:11896189 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C1704319 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C1412459 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C1752722 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
| pubmed-article:11896189 | lifeskim:mentions | umls-concept:C2353566 | lld:lifeskim |
| pubmed-article:11896189 | pubmed:issue | Pt 7 | lld:pubmed |
| pubmed-article:11896189 | pubmed:dateCreated | 2002-3-15 | lld:pubmed |
| pubmed-article:11896189 | pubmed:abstractText | The multigenic family of mammalian Fe65s encodes three highly similar proteins with the same modular organisation: a WW domain and two phosphotyrosine-binding domains. The PTB2 domain of these proteins binds to the cytosolic domains of the Alzheimer's beta-amyloid precursor protein APP and related proteins APLP1 and APLP2, generating a highly redundant system that is hard to dissect by reverse genetics. By searching potential Fe65-like genes in the nematode Caenorhabditis elegans, we identified a single gene, feh-1 (Fe65 homolog-1), encoding a protein with a high sequence similarity to mammalian Fe65s. FEH-1 is also functionally related to mammalian orthologues; in fact its PTB2 domain binds to APL-1, the product of the C. elegans orthologue of APP. Staining with specific antibodies show that the neuromuscular structures of the pharynx are the sites in which FEH-1 is present at highest levels. Expression studies with reporters indicate that the feh-1 gene is also expressed by a subset of the worm neurons. We generated and isolated a deletion allele of feh-1, and the corresponding homozygous mutants arrest as late embryos or as L1 larvae, demonstrating for the first time an essential role for a Fe65-like gene in vivo. The pharynx of homozygous larvae does not contract and the worms cannot feed. Analysis of pharyngeal pumping in heterozygous worms and in feh-1 RNA-interfered worms indicates that dosage of feh-1 function affects the rate of pharyngeal contraction in C. elegans. Interference with apl-1 double-stranded RNA showed a similar effect on pharyngeal pumping, suggesting that FEH-1 and APL-1 are involved in the same pathway. The non-redundant system of the nematode will prove useful for studying the basic biology of the Fe65-APP interaction and the molecular events regulated by this evolutionarily conserved system of interacting proteins. | lld:pubmed |
| pubmed-article:11896189 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11896189 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11896189 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11896189 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11896189 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11896189 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11896189 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11896189 | pubmed:issn | 0021-9533 | lld:pubmed |
| pubmed-article:11896189 | pubmed:author | pubmed-author:RussoTommasoT | lld:pubmed |
| pubmed-article:11896189 | pubmed:author | pubmed-author:BazzicalupoPa... | lld:pubmed |
| pubmed-article:11896189 | pubmed:author | pubmed-author:ArbucciSalvat... | lld:pubmed |
| pubmed-article:11896189 | pubmed:author | pubmed-author:ZambranoNicol... | lld:pubmed |
| pubmed-article:11896189 | pubmed:author | pubmed-author:BimonteMarida... | lld:pubmed |
| pubmed-article:11896189 | pubmed:author | pubmed-author:GianniDavideD | lld:pubmed |
| pubmed-article:11896189 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11896189 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11896189 | pubmed:volume | 115 | lld:pubmed |
| pubmed-article:11896189 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11896189 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11896189 | pubmed:pagination | 1411-22 | lld:pubmed |
| pubmed-article:11896189 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11896189 | pubmed:meshHeading | pubmed-meshheading:11896189... | lld:pubmed |
| pubmed-article:11896189 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11896189 | pubmed:articleTitle | feh-1 and apl-1, the Caenorhabditis elegans orthologues of mammalian Fe65 and beta-amyloid precursor protein genes, are involved in the same pathway that controls nematode pharyngeal pumping. | lld:pubmed |
| pubmed-article:11896189 | pubmed:affiliation | Dipartimento di Biochimica e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, Via S. Pansini, 5, I-80131, Napoli, Italy. zambrano@unina.it | lld:pubmed |
| pubmed-article:11896189 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11896189 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:11896189 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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