Absence of a carbohydrate modification does not affect the level or subcellular localization of three membrane glycoproteins in modB mutants of Dictyostelium discoideum.
The accumulation and localization of four developmentally regulated membrane glycoproteins were examined in a glycosylation mutant of the cellular slime mold Dictyostelium discoideum. As judged by immunoblot procedures using antipeptide antibodies, the levels of three of the glycoproteins, WGA80B, SP29A, and SP29B, were unaffected, but their apparent molecular masses were reduced by 14,000, 3,500 and 3,500 daltons, respectively. The level of the fourth glycoprotein, gp80, was reduced to below detectable limits. The reduced molecular sizes were apparently due to the absence of certain carbohydrate structures as judged by labeling Western blots with anti-carbohydrate antibodies and a lectin. Using immunofluorescence labeling of permeabilized and intact cells, the localization of WGA80B, SP29A, and SP29B, in intracellular vesicles and on the cell surface of prespore cells, was observed to be unaffected in the mutant cells. The developmentally regulated oligosaccharide structure(s) affected by the modB locus does not influence the subcellular localization and accumulation of these three glycoproteins in the prespore cells of this phylogenetically primitive organism.
D000818:Animals; D002241:Carbohydrates / Q000502:physiology*; D004023:Dictyostelium / Q000032:analysis*; D005455:Fluorescent Antibody Technique; D005656:Fungal Proteins / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis* / Q000276:immunology; D008565:Membrane Proteins / Q000032:analysis*; D051379:Mice; D009154:Mutation; D011817:Rabbits
D002241:Carbohydrates; D005656:Fungal Proteins; D006023:Glycoproteins; D008565:Membrane Proteins