Author(s): Nombela C, Gil C, Chaffin WL
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Abstract Many proteins are transported to the cell surface of Saccharomyces cerevisiae and Candida albicans to be either integrated into the cell-wall structure or exported to the external medium. Secretion of many of these proteins through the classical endoplasmic reticulum-Golgi pathway is driven by a canonical N-terminal signal peptide. However, several surface proteins lacking this motif can also access the cell surface and remain loosely bound to the wall. The previous identification of these secretion-signal-less proteins in the cytoplasm as proteins that function as glycolytic enzymes, chaperones, translation factors and others suggests that they could be "moonlighting" (multifunctional) proteins. The accumulated evidence indicates that mechanisms of secretion other than the endoplasmic reticulum-Golgi pathway drive these proteins outside the plasma membrane. The relevance of these secretion-signal-less proteins in virulence and cell-wall dynamics warrants further characterization of alternative secretion in yeasts.
This article was published in Trends Microbiol
and referenced in Journal of Clinical & Experimental Pharmacology