PubMed:11483512 JSONTXT

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":10,"end":15},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T2","span":{"begin":86,"end":90},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"T3","span":{"begin":95,"end":99},"obj":"https://acgg.asia/db/ggdb/info/gg230"},{"id":"T4","span":{"begin":558,"end":562},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"T5","span":{"begin":567,"end":571},"obj":"https://acgg.asia/db/ggdb/info/gg230"},{"id":"T6","span":{"begin":634,"end":639},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T7","span":{"begin":674,"end":679},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T8","span":{"begin":763,"end":768},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T9","span":{"begin":923,"end":928},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T10","span":{"begin":957,"end":961},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"T11","span":{"begin":966,"end":970},"obj":"https://acgg.asia/db/ggdb/info/gg230"},{"id":"T12","span":{"begin":981,"end":986},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T13","span":{"begin":1042,"end":1046},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"T14","span":{"begin":1051,"end":1055},"obj":"https://acgg.asia/db/ggdb/info/gg230"},{"id":"T15","span":{"begin":1139,"end":1144},"obj":"https://acgg.asia/db/ggdb/info/gg233"}],"text":"PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8.\nMany 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."}

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{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":10,"end":15},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T2","span":{"begin":86,"end":90},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"T3","span":{"begin":95,"end":99},"obj":"https://acgg.asia/db/ggdb/info/gg230"},{"id":"T4","span":{"begin":558,"end":562},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"T5","span":{"begin":567,"end":571},"obj":"https://acgg.asia/db/ggdb/info/gg230"},{"id":"T6","span":{"begin":634,"end":639},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T7","span":{"begin":674,"end":679},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T8","span":{"begin":763,"end":768},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T9","span":{"begin":923,"end":928},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T10","span":{"begin":957,"end":961},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"T11","span":{"begin":966,"end":970},"obj":"https://acgg.asia/db/ggdb/info/gg230"},{"id":"T12","span":{"begin":981,"end":986},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"T13","span":{"begin":1042,"end":1046},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"T14","span":{"begin":1051,"end":1055},"obj":"https://acgg.asia/db/ggdb/info/gg230"},{"id":"T15","span":{"begin":1139,"end":1144},"obj":"https://acgg.asia/db/ggdb/info/gg233"}],"text":"PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8.\nMany 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."}

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{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":0,"end":3},"obj":"https://acgg.asia/db/ggdb/info/gg232"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":10,"end":15},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":86,"end":90},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":558,"end":562},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":624,"end":627},"obj":"https://acgg.asia/db/ggdb/info/gg232"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":634,"end":639},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":664,"end":667},"obj":"https://acgg.asia/db/ggdb/info/gg232"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":674,"end":679},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":753,"end":756},"obj":"https://acgg.asia/db/ggdb/info/gg232"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":763,"end":768},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":913,"end":916},"obj":"https://acgg.asia/db/ggdb/info/gg232"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":923,"end":928},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":957,"end":961},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"PD-GlycoGenes20190927-B_T14","span":{"begin":981,"end":986},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"PD-GlycoGenes20190927-B_T15","span":{"begin":1042,"end":1046},"obj":"https://acgg.asia/db/ggdb/info/gg231"},{"id":"PD-GlycoGenes20190927-B_T16","span":{"begin":1139,"end":1144},"obj":"https://acgg.asia/db/ggdb/info/gg233"},{"id":"PD-GlycoGenes20190927-B_T17","span":{"begin":1149,"end":1152},"obj":"https://acgg.asia/db/ggdb/info/gg232"}],"text":"PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8.\nMany 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."}