title: Cisterna-specific localization of glycosylation-related proteins to the Golgi apparatus.
abstract: The Golgi apparatus is an intracellular organelle playing central roles in post-translational modification and in the secretion of membrane and secretory proteins. These proteins are synthesized in the endoplasmic reticulum (ER) and transported to the cis-, medial-and trans-cisternae of the Golgi. While trafficking through the Golgi, proteins are sequentially modified with glycan moieties by different glycosyltransferases. Therefore, it is important to analyze the glycosylation function of the Golgi at the level of cisternae. Markers widely used for cis-, medial- and trans-cisternae/trans Golgi network (TGN) in Drosophila are GM130, 120 kDa and Syntaxin16 (Syx16); however the anti-120 kDa antibody is no longer available. In the present study, Drosophila Golgi complex-localized glycoprotein-1 (dGLG1) was identified as an antigen recognized by the anti-120 kDa antibody. A monoclonal anti-dGLG1 antibody suitable for immunohistochemistry was raised in rat. Using these markers, the localization of glycosyltransferases and nucleotide-sugar transporters (NSTs) was studied at the cisternal level. Results showed that glycosyltransferases and NSTs involved in the same sugar modification are localized to the same cisternae. Furthermore, valuable functional information was obtained on the localization of novel NSTs with as yet incompletely characterized biochemical properties.
authors.affiliation: Department of Physiology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo, Japan..
authors.forename: Miki
authors.initials: M
authors.lastname: Yamamoto-Hino
authors.forename: Masato
authors.initials: M
authors.lastname: Abe
authors.forename: Takako
authors.initials: T
authors.lastname: Shibano
authors.forename: Yuka
authors.initials: Y
authors.lastname: Setoguchi
authors.forename: Wakae
authors.initials: W
authors.lastname: Awano
authors.forename: Ryu
authors.initials: R
authors.lastname: Ueda
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Okano
authors.forename: Satoshi
authors.initials: S
authors.lastname: Goto
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D001692:Biological Transport; D015415:Biomarkers; D002478:Cells, Cultured; D029721:Drosophila Proteins / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000166:cytology / Q000378:metabolism*; D006031:Glycosylation; D016695:Glycosyltransferases / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D011499:Protein Processing, Post-Translational; D051381:Rats; D017468:Receptors, Fibroblast Growth Factor / Q000096:biosynthesis* / Q000276:immunology; D012795:Sialoglycoproteins / Q000096:biosynthesis* / Q000276:immunology
chemical_list: D000911:Antibodies, Monoclonal; D015415:Biomarkers; D029721:Drosophila Proteins; D017468:Receptors, Fibroblast Growth Factor; D012795:Sialoglycoproteins; C086711:cysteine-rich fibroblast growth factor receptor; D016695:Glycosyltransferases