title: Glycosylation of tetraspanin Tspan-1 at four distinct sites promotes its transition through the endoplasmic reticulum.
abstract: We showed that Tspan-1, a tetraspanin overexpressed in many human cancers, harbours oligosaccharides at all four potential N-glycosylation sites. Its most abundant form contained only mannose-rich sugar chains but two distinct glycosylation sites could also contain complex carbohydrates. Glycosylation seemed to be required for correct folding and subsequent transition through the endoplasmic reticulum.
authors.affiliation: Department of Obstetrics and Gynaecology, University of Ulm, Germany.
authors.forename: Claus-Jürgen
authors.initials: CJ
authors.lastname: Scholz
authors.forename: Georg
authors.initials: G
authors.lastname: Sauer
authors.forename: Helmut
authors.initials: H
authors.lastname: Deissler
mesh_terms: D001665:Binding Sites / Q000235:genetics; D045744:Cell Line, Tumor; D002462:Cell Membrane / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005260:Female; D006031:Glycosylation; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D015151:Immunoblotting; D008247:Lysosomes / Q000378:metabolism; D008358:Mannose / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D009154:Mutation; D009844:Oligosaccharides / Q000378:metabolism; D010051:Ovarian Neoplasms / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D017510:Protein Folding; D021381:Protein Transport; D059470:Tetraspanins; D014162:Transfection
chemical_list: D008565:Membrane Proteins; D009844:Oligosaccharides; C508125:TSPAN1 protein, human; D059470:Tetraspanins; D049452:Green Fluorescent Proteins; D008358:Mannose