| pubmed-article:16278447 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C0061688 | lld:lifeskim |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C0205265 | lld:lifeskim |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C1555582 | lld:lifeskim |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:16278447 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:16278447 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:16278447 | pubmed:dateCreated | 2005-11-9 | lld:pubmed |
| pubmed-article:16278447 | pubmed:abstractText | Glycosylphosphatidylinositols (GPIs) are attached to the C termini of some glycosylated secretory proteins, serving as membrane anchors for many of those on the cell surface. Biosynthesis of GPIs is initiated by the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to phosphatidylinositol. This reaction is carried out at the endoplasmic reticulum (ER) by an enzyme complex called GPI-N-acetylglucosaminyltransferase (GPI-GlcNAc transferase). The human enzyme has six known subunits, at least four of which, GPI1, PIG-A, PIG-C, and PIG-H, have functional homologs in the budding yeast Saccharomyces cerevisiae. The uncharacterized yeast gene YDR437w encodes a protein with some sequence similarity to human PIG-P, a fifth subunit of the GPI-GlcNAc transferase. Here we show that Ydr437w is a small but essential subunit of the yeast GPI-GlcNAc transferase, and we designate its gene GPI19. Similar to other mutants in the yeast enzyme, temperature-sensitive gpi19 mutants display cell wall defects and hyperactive Ras phenotypes. The Gpi19 protein associates with the yeast GPI-GlcNAc transferase in vivo, as judged by coimmuneprecipitation with the Gpi2 subunit. Moreover, conditional gpi19 mutants are defective for GPI-GlcNAc transferase activity in vitro. Finally, we present evidence for the topology of Gpi19 within the ER membrane. | lld:pubmed |
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| pubmed-article:16278447 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16278447 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16278447 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16278447 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16278447 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16278447 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16278447 | pubmed:issn | 1535-9778 | lld:pubmed |
| pubmed-article:16278447 | pubmed:author | pubmed-author:OrleanPeterP | lld:pubmed |
| pubmed-article:16278447 | pubmed:author | pubmed-author:LewisSarah... | lld:pubmed |
| pubmed-article:16278447 | pubmed:author | pubmed-author:RomeoMartin... | lld:pubmed |
| pubmed-article:16278447 | pubmed:author | pubmed-author:LevinDavid... | lld:pubmed |
| pubmed-article:16278447 | pubmed:author | pubmed-author:YanBenjamin... | lld:pubmed |
| pubmed-article:16278447 | pubmed:author | pubmed-author:NewmanHeather... | lld:pubmed |
| pubmed-article:16278447 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16278447 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:16278447 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16278447 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16278447 | pubmed:pagination | 1801-7 | lld:pubmed |
| pubmed-article:16278447 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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