PubMed:9724629 JSONTXT

{"project":"ggdb-test","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T2","span":{"begin":132,"end":136},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T3","span":{"begin":484,"end":488},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T4","span":{"begin":651,"end":655},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T5","span":{"begin":742,"end":746},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T6","span":{"begin":783,"end":787},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T7","span":{"begin":889,"end":893},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T8","span":{"begin":961,"end":965},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T9","span":{"begin":977,"end":981},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T10","span":{"begin":1061,"end":1065},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T11","span":{"begin":1107,"end":1111},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T12","span":{"begin":1172,"end":1176},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T13","span":{"begin":1244,"end":1248},"obj":"https://acgg.asia/db/ggdb/info/gg203"}],"text":"DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate.\nBiosynthesis of glycosylphosphatidylinositol and N-glycan precursor is dependent upon a mannosyl donor, dolichol phosphate-mannose (DPM). The Thy-1negative class E mutant of mouse lymphoma and Lec15 mutant Chinese hamster ovary (CHO) cells are incapable of DPM synthesis. The class E mutant is defective in the DPM1 gene which encodes a mammalian homologue of Saccharomyces cerevisiae Dpm1p that is a DPM synthase, whereas Lec15 is a different mutant, indicating that mammalian DPM1 is not sufficient for DPM synthesis. Here we report expression cloning of a new gene, DPM2, which is defective in Lec15 cells. DPM2, an 84 amino acid membrane protein expressed in the endoplasmic reticulum (ER), makes a complex with DPM1 that is essential for the ER localization and stable expression of DPM1. Moreover, DPM2 enhances binding of dolichol phosphate, a substrate of DPM synthase. Mammalian DPM1 is catalytic because a fusion protein of DPM1 that was stably expressed in the ER synthesized DPM without DPM2. Therefore, biosynthesis of DPM in mammalian cells is regulated by DPM2."}

{"project":"GGDB-2020","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T2","span":{"begin":132,"end":136},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T3","span":{"begin":484,"end":488},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T4","span":{"begin":651,"end":655},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T5","span":{"begin":742,"end":746},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T6","span":{"begin":783,"end":787},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T7","span":{"begin":889,"end":893},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T8","span":{"begin":961,"end":965},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T9","span":{"begin":977,"end":981},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T10","span":{"begin":1061,"end":1065},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T11","span":{"begin":1107,"end":1111},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"T12","span":{"begin":1172,"end":1176},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"T13","span":{"begin":1244,"end":1248},"obj":"https://acgg.asia/db/ggdb/info/gg203"}],"text":"DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate.\nBiosynthesis of glycosylphosphatidylinositol and N-glycan precursor is dependent upon a mannosyl donor, dolichol phosphate-mannose (DPM). The Thy-1negative class E mutant of mouse lymphoma and Lec15 mutant Chinese hamster ovary (CHO) cells are incapable of DPM synthesis. The class E mutant is defective in the DPM1 gene which encodes a mammalian homologue of Saccharomyces cerevisiae Dpm1p that is a DPM synthase, whereas Lec15 is a different mutant, indicating that mammalian DPM1 is not sufficient for DPM synthesis. Here we report expression cloning of a new gene, DPM2, which is defective in Lec15 cells. DPM2, an 84 amino acid membrane protein expressed in the endoplasmic reticulum (ER), makes a complex with DPM1 that is essential for the ER localization and stable expression of DPM1. Moreover, DPM2 enhances binding of dolichol phosphate, a substrate of DPM synthase. Mammalian DPM1 is catalytic because a fusion protein of DPM1 that was stably expressed in the ER synthesized DPM without DPM2. Therefore, biosynthesis of DPM in mammalian cells is regulated by DPM2."}

{"project":"glycogenes","denotations":[{"id":"PD-GlycoGenes20190927-B_T1","span":{"begin":0,"end":4},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"PD-GlycoGenes20190927-B_T2","span":{"begin":132,"end":136},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"PD-GlycoGenes20190927-B_T3","span":{"begin":484,"end":488},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"PD-GlycoGenes20190927-B_T4","span":{"begin":651,"end":655},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"PD-GlycoGenes20190927-B_T5","span":{"begin":742,"end":746},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"PD-GlycoGenes20190927-B_T6","span":{"begin":783,"end":787},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"PD-GlycoGenes20190927-B_T7","span":{"begin":889,"end":893},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"PD-GlycoGenes20190927-B_T8","span":{"begin":961,"end":965},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"PD-GlycoGenes20190927-B_T9","span":{"begin":977,"end":981},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"PD-GlycoGenes20190927-B_T10","span":{"begin":1061,"end":1065},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"PD-GlycoGenes20190927-B_T11","span":{"begin":1107,"end":1111},"obj":"https://acgg.asia/db/ggdb/info/gg140"},{"id":"PD-GlycoGenes20190927-B_T12","span":{"begin":1172,"end":1176},"obj":"https://acgg.asia/db/ggdb/info/gg203"},{"id":"PD-GlycoGenes20190927-B_T13","span":{"begin":1244,"end":1248},"obj":"https://acgg.asia/db/ggdb/info/gg203"}],"text":"DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate.\nBiosynthesis of glycosylphosphatidylinositol and N-glycan precursor is dependent upon a mannosyl donor, dolichol phosphate-mannose (DPM). The Thy-1negative class E mutant of mouse lymphoma and Lec15 mutant Chinese hamster ovary (CHO) cells are incapable of DPM synthesis. The class E mutant is defective in the DPM1 gene which encodes a mammalian homologue of Saccharomyces cerevisiae Dpm1p that is a DPM synthase, whereas Lec15 is a different mutant, indicating that mammalian DPM1 is not sufficient for DPM synthesis. Here we report expression cloning of a new gene, DPM2, which is defective in Lec15 cells. DPM2, an 84 amino acid membrane protein expressed in the endoplasmic reticulum (ER), makes a complex with DPM1 that is essential for the ER localization and stable expression of DPM1. Moreover, DPM2 enhances binding of dolichol phosphate, a substrate of DPM synthase. Mammalian DPM1 is catalytic because a fusion protein of DPM1 that was stably expressed in the ER synthesized DPM without DPM2. Therefore, biosynthesis of DPM in mammalian cells is regulated by DPM2."}