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- W2890315538 endingPage "2736" @default.
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- W2890315538 abstract "To observe internalization of the yeast pheromone receptor Ste2 by fluorescence microscopy in live cells in real time, we visualized only those molecules present at the cell surface at the time of agonist engagement (rather than the total cellular pool) by tagging this receptor at its N-terminus with an exocellular fluorogen-activating protein (FAP). A FAP is a single-chain antibody engineered to bind tightly a nonfluorescent, cell-impermeable dye (fluorogen), thereby generating a fluorescent complex. The utility of FAP tagging to study trafficking of integral membrane proteins in yeast, which possesses a cell wall, had not been examined previously. A diverse set of signal peptides and propeptide sequences were explored to maximize expression. Maintenance of the optimal FAP-Ste2 chimera intact required deletion of two, paralogous, glycosylphosphatidylinositol (GPI)-anchored extracellular aspartyl proteases (Yps1 and Mkc7). FAP-Ste2 exhibited a much brighter and distinct plasma membrane signal than Ste2-GFP or Ste2-mCherry yet behaved quite similarly. Using FAP-Ste2, new information was obtained about the mechanism of its internalization, including novel insights about the roles of the cargo-selective endocytic adaptors Ldb19/Art1, Rod1/Art4, and Rog3/Art7." @default.
- W2890315538 created "2018-09-27" @default.
- W2890315538 creator A5033717510 @default.
- W2890315538 creator A5036193748 @default.
- W2890315538 creator A5041068764 @default.
- W2890315538 creator A5048920959 @default.
- W2890315538 date "2018-11-01" @default.
- W2890315538 modified "2023-10-13" @default.
- W2890315538 title "Tracking yeast pheromone receptor Ste2 endocytosis using fluorogen-activating protein tagging" @default.
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