| pubmed-article:12639958 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12639958 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:12639958 | lifeskim:mentions | umls-concept:C0002812 | lld:lifeskim |
| pubmed-article:12639958 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:12639958 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:12639958 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:12639958 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:12639958 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:12639958 | lifeskim:mentions | umls-concept:C0379528 | lld:lifeskim |
| pubmed-article:12639958 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:12639958 | pubmed:dateCreated | 2003-5-26 | lld:pubmed |
| pubmed-article:12639958 | pubmed:abstractText | PEN-2 is an integral membrane protein that is a necessary component of the gamma-secretase complex, which is central in the pathogenesis of Alzheimer's disease and is also required for Notch signaling. In the absence of PEN-2, Notch signaling fails to guide normal development in Caenorhabditis elegans, and amyloid beta peptide is not generated from the amyloid precursor protein. Human PEN-2 is a 101-amino acid protein containing two putative transmembrane domains. To understand its interaction with other gamma-secretase components, it is important to know the membrane topology of each member of the complex. To characterize the membrane topology of PEN-2, we introduced single amino acid changes in each of the three hydrophilic regions of PEN-2 to generate N-linked glycosylation sites. We found that the N-linked glycosylation sites present in the N- and C-terminal domains of PEN-2 were utilized, whereas a site in the hydrophilic "loop" region connecting the two transmembrane domains was not. The addition of a carbohydrate structure in the N-terminal domain of PEN-2 prevented association with presenilin 1, whereas glycosylation in the C-terminal region of PEN-2 did not, suggesting that the N-terminal domain is important for interactions with presenilin 1. Immunofluorescence microscopy with selective permeabilization of the plasma membrane of cells expressing epitope-tagged forms of PEN-2 confirmed the lumenal location of both the N and C termini. A protease protection assay also demonstrated that the loop domain of PEN-2 is cytosolic. Thus, PEN-2 spans the membrane twice, with the N and C termini facing the lumen of the endoplasmic reticulum. | lld:pubmed |
| pubmed-article:12639958 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12639958 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12639958 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12639958 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12639958 | pubmed:month | May | lld:pubmed |
| pubmed-article:12639958 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12639958 | pubmed:author | pubmed-author:LeeVirginia... | lld:pubmed |
| pubmed-article:12639958 | pubmed:author | pubmed-author:DomsRobert... | lld:pubmed |
| pubmed-article:12639958 | pubmed:author | pubmed-author:CarlinDanD | lld:pubmed |
| pubmed-article:12639958 | pubmed:author | pubmed-author:PijakDonald... | lld:pubmed |
| pubmed-article:12639958 | pubmed:author | pubmed-author:PiersonTheodo... | lld:pubmed |
| pubmed-article:12639958 | pubmed:author | pubmed-author:MoraisVanessa... | lld:pubmed |
| pubmed-article:12639958 | pubmed:author | pubmed-author:CrystalAdam... | lld:pubmed |
| pubmed-article:12639958 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12639958 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:12639958 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12639958 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12639958 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12639958 | pubmed:pagination | 20117-23 | lld:pubmed |
| pubmed-article:12639958 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12639958 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12639958 | pubmed:articleTitle | Membrane topology of gamma-secretase component PEN-2. | lld:pubmed |
| pubmed-article:12639958 | pubmed:affiliation | Department of Microbiology, The Center for Neurodegenerative Disease Research, University of Pennsylvania School of Medicine, Philadelphia 19104, USA. | lld:pubmed |
| pubmed-article:12639958 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12639958 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12639958 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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