« Previous AbstractExploitation of a microporous organic polymer as a stationary phase for capillary gas chromatography    Next AbstractMulti-adsorbent preconcentration/focusing module for portable-GC/microsensor-array analysis of complex vapor mixtures »

J Cell Biol

Title:		"Glycosyl phosphatidylinositol-dependent cross-linking of alpha-agglutinin and beta 1,6-glucan in the Saccharomyces cerevisiae cell wall"
Author(s):		Lu CF; Montijn RC; Brown JL; Klis F; Kurjan J; Bussey H; Lipke PN;
Address:		"Department of Biological Sciences, Hunter College of the City University of New York, New York 10021"
Journal Title:		J Cell Biol
Year:		1995
Volume:		128
Issue:		3
Page Number:		333 - 340
DOI:		10.1083/jcb.128.3.333
ISSN/ISBN:		0021-9525 (Print) 1540-8140 (Electronic) 0021-9525 (Linking)
Abstract:		"The cell adhesion protein alpha-agglutinin is bound to the outer surface of the Saccharomyces cerevisiae cell wall and mediates cell-cell contact in mating. alpha-Agglutinin is modified by addition of a glycosyl phosphatidylinositol (GPI) anchor as it traverses the secretory pathway. The presence of a GPI anchor is essential for cross-linking into the wall, but the fatty acid and inositol components of the anchor are lost before cell wall association (Lu, C.-F., J. Kurjan, and P. N. Lipke, 1994. A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin. Mol. Cell. Biol. 14:4825-4833). Cell wall association of alpha-agglutinin was accompanied by an increase in size and a gain in reactivity to antibodies directed against beta 1,6-glucan. Several kre mutants, which have defects in synthesis of cell wall beta 1,6-glucan, had reduced molecular size of cell wall alpha-agglutinin. These findings demonstrate that the cell wall form of alpha-agglutinin is covalently associated with beta 1,6-glucan. The alpha-agglutinin biosynthetic precursors did not react with antibody to beta 1,6-glucan, and the sizes of these forms were unaffected in kre mutants. A COOH-terminal truncated form of alpha-agglutinin, which is not GPI anchored and is secreted into the medium, did not react with the anti-beta 1,6-glucan. We propose that extracellular cross-linkage to beta 1,6-glucan mediates covalent association of alpha-agglutinin with the cell wall in a manner that is dependent on prior addition of a GPI anchor to alpha-agglutinin"
Keywords:		Antibodies/immunology Cell Adhesion Cell Wall/metabolism Glucans/immunology/*metabolism Glycosylphosphatidylinositols/*metabolism Mating Factor Mutation Particle Size Peptides/*metabolism Saccharomyces cerevisiae/*metabolism *beta-Glucans;
Notes:		"MedlineLu, C F Montijn, R C Brown, J L Klis, F Kurjan, J Bussey, H Lipke, P N eng Research Support, Non-U.S. Gov't 1995/02/01 J Cell Biol. 1995 Feb; 128(3):333-40. doi: 10.1083/jcb.128.3.333"