| Title: | A biochemical guide to yeast adhesins: glycoproteins for social and antisocial occasions |
| Author(s): | Dranginis AM; Rauceo JM; Coronado JE; Lipke PN; |
| Address: | "Department of Biological Science, St John's University, Queens, New York, USA" |
| ISSN/ISBN: | 1092-2172 (Print) 1098-5557 (Electronic) 1092-2172 (Linking) |
| Abstract: | "Fungi are nonmotile eukaryotes that rely on their adhesins for selective interaction with the environment and with other fungal cells. Glycosylphosphatidylinositol (GPI)-cross-linked adhesins have essential roles in mating, colony morphology, host-pathogen interactions, and biofilm formation. We review the structure and binding properties of cell wall-bound adhesins of ascomycetous yeasts and relate them to their effects on cellular interactions, with particular emphasis on the agglutinins and flocculins of Saccharomyces and the Als proteins of Candida. These glycoproteins share common structural motifs tailored to surface activity and biological function. After being secreted to the outer face of the plasma membrane, they are covalently anchored in the wall through modified GPI anchors, with their binding domains elevated beyond the wall surface on highly glycosylated extended stalks. N-terminal globular domains bind peptide or sugar ligands, with between millimolar and nanomolar affinities. These affinities and the high density of adhesins and ligands at the cell surface determine microscopic and macroscopic characteristics of cell-cell associations. Central domains often include Thr-rich tandemly repeated sequences that are highly glycosylated. These domains potentiate cell-to-cell binding, but the molecular mechanism of such an association is not yet clear. These repeats also mediate recombination between repeats and between genes. The high levels of recombination and epigenetic regulation are sources of variation which enable the population to continually exploit new niches and resources" |
| Keywords: | Cell Adhesion/physiology Cell Adhesion Molecules/physiology Glycoproteins/*physiology Mating Factor Peptides/physiology Pheromones/physiology Saccharomyces cerevisiae/genetics/*physiology; |
| Notes: | "MedlineDranginis, Anne M Rauceo, Jason M Coronado, Juan E Lipke, Peter N eng S06 GM060654/GM/NIGMS NIH HHS/ F31 GM 070122/GM/NIGMS NIH HHS/ F31 GM070122/GM/NIGMS NIH HHS/ S06 GM076168/GM/NIGMS NIH HHS/ RR03037/RR/NCRR NIH HHS/ R15 AI 43927/AI/NIAID NIH HHS/ G12 RR003037/RR/NCRR NIH HHS/ S06 GM60654/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Review 2007/06/08 Microbiol Mol Biol Rev. 2007 Jun; 71(2):282-94. doi: 10.1128/MMBR.00037-06" |
