Title: | A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin |
Author(s): | Lu CF; Kurjan J; Lipke PN; |
Address: | "Department of Biological Sciences, Hunter College, City University of New York, New York 10021" |
DOI: | 10.1128/mcb.14.7.4825-4833.1994 |
ISSN/ISBN: | 0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking) |
Abstract: | "Saccharomyces cerevisiae alpha-agglutinin is a cell wall-anchored adhesion glycoprotein. The previously identified 140-kDa form, which contains a glycosyl-phosphatidylinositol (GPI) anchor (D. Wojciechowicz, C.-F. Lu, J. Kurjan, and P. N. Lipke, Mol. Cell. Biol. 13:2554-2563, 1993), and additional forms of 80, 150, 250 to 300, and > 300 kDa had the properties of intermediates in a transport and cell wall anchorage pathway. N glycosylation and additional modifications resulted in successive increases in size during transport. The 150- and 250- to 300-kDa forms were membrane associated and are likely to be intermediates between the 140-kDa form and a cell surface GPI-anchored form of > 300 kDa. A soluble form of > 300 kDa that lacked the GPI anchor had properties of a periplasmic intermediate between the plasma membrane form and the > 300-kDa cell wall-anchored form. These results constitute experimental support for the hypothesis that GPI anchors act to localize alpha-agglutinin to the plasma membrane and that cell wall anchorage involves release from the GPI anchor to produce a periplasmic intermediate followed by linkage to the cell wall" |
Keywords: | "Cell Wall/*physiology Endopeptidase K Glucan Endo-1, 3-beta-D-Glucosidase/metabolism Glycosylphosphatidylinositols/metabolism Inositol/metabolism Kinetics Mating Factor Membrane Glycoproteins/*biosynthesis/isolation & purification Methionine/metabolism Mol;" |
Notes: | "MedlineLu, C F Kurjan, J Lipke, P N eng Research Support, U.S. Gov't, P.H.S. 1994/07/01 Mol Cell Biol. 1994 Jul; 14(7):4825-33. doi: 10.1128/mcb.14.7.4825-4833.1994" |