| pubmed-article:11483512 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C1314972 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C1333690 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C1415190 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C1418566 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C0237497 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C0185023 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C1947904 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C1999228 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C2825781 | lld:lifeskim |
| pubmed-article:11483512 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:11483512 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:11483512 | pubmed:dateCreated | 2001-8-2 | lld:pubmed |
| pubmed-article:11483512 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:abstractText | Many eukaryotic cell surface proteins are anchored to the plasma membrane via glycosylphosphatidylinositol (GPI). The GPI transamidase mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with a substrate protein. It was known that the GPI transamidase is a complex containing GAA1 and GPI8. Here, we report two new components of this enzyme: PIG-S and PIG-T. To determine roles for PIG-S and PIG-T, we disrupted these genes in mouse F9 cells by homologous recombination. PIG-S and PIG-T knockout cells were defective in transfer of GPI to proteins, particularly in formation of the carbonyl intermediates. We also demonstrate that PIG-S and PIG-T form a protein complex with GAA1 and GPI8, and that PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8. Saccharomyces cerevisiae Gpi16p (YHR188C) and Gpi17p (YDR434W) are orthologues of PIG-T and PIG-S, respectively. | lld:pubmed |
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| pubmed-article:11483512 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11483512 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11483512 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11483512 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:11483512 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11483512 | pubmed:author | pubmed-author:InoueNN | lld:pubmed |
| pubmed-article:11483512 | pubmed:author | pubmed-author:KinoshitaTT | lld:pubmed |
| pubmed-article:11483512 | pubmed:author | pubmed-author:OhishiKK | lld:pubmed |
| pubmed-article:11483512 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11483512 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11483512 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:11483512 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11483512 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11483512 | pubmed:pagination | 4088-98 | lld:pubmed |
| pubmed-article:11483512 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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