| http://purl.uniprot.org/citations/19420140 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19420140 | http://www.w3.org/2000/01/rdf-schema#comment | "GM3 synthase (SAT-I) is the primary glycosyltransferase responsible for the biosynthesis of ganglio-series gangliosides. In this study, we identify three isoforms of mouse SAT-I proteins, named M1-SAT-I, M2-SAT-I, and M3-SAT-I, which possess distinct lengths in their NH(2)-terminal cytoplasmic tails. These isoforms are produced by leaky scanning from mRNA variants of mSAT-Ia and mSAT-Ib. M2-SAT-I and M3-SAT-I were found to be localized in the Golgi apparatus, as expected, whereas M1-SAT-I was exclusively found in the endoplasmic reticulum (ER). Specific multiple arginines (R) arranged in an R-based motif, RRXXXXR necessary for ER targeting, were found in the cytoplasmic tail of M1-SAT-I, and in vivo GM3 biosynthesis by M1-SAT-I was very low because of restricted transport to the Golgi apparatus. In addition, M1-SAT-I and M3-SAT-I had a long half-life relative to M2-SAT-I. This is the first report demonstrating the presence of an ER-targeting R-based motif in the cytoplasmic tail of a protein in the mammalian glycosyltransferase family of enzymes. The system, which produces SAT-I isoforms having distinct characteristics, is likely to be of critical importance for the regulation of GM3 biosynthesis under various pathological and physiological conditions."xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e08-12-1219"xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/author | "Yoshida S."xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/author | "Inokuchi J."xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/author | "Uemura S."xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/author | "Shishido F."xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/name | "Mol Biol Cell"xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/pages | "3088-3100"xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/title | "The cytoplasmic tail of GM3 synthase defines its subcellular localization, stability, and in vivo activity."xsd:string |
| http://purl.uniprot.org/citations/19420140 | http://purl.uniprot.org/core/volume | "20"xsd:string |
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