Glycosylation of tetraspanin Tspan-1 at four distinct sites promotes its transition through the endoplasmic reticulum.
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.
Scholz
Claus-Jürgen
CJ
Department of Obstetrics and Gynaecology, University of Ulm, Germany.
Sauer
Georg
G
Deissler
Helmut
H
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
D008565:Membrane Proteins; D009844:Oligosaccharides; C508125:TSPAN1 protein, human; D059470:Tetraspanins; D049452:Green Fluorescent Proteins; D008358:Mannose