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• W2007580201 abstract "Abstract Protein localization is tightly linked with function, such that the subcellular distribution of a protein serves as an important control point regulating activity. Exploiting this regulatory mechanism, we present here a general approach by which protein location, and hence function, may be controlled on demand in the budding yeast. In this system a small molecule, rapamycin, is used to temporarily recruit a strong cellular address signal to the target protein, placing subcellular localization under control of the selective chemical stimulus. The kinetics of this system are rapid: rapamycin‐directed nucleo‐cytoplasmic transport is evident 10–12 min post‐treatment and the process is reversible upon removal of rapamycin. Accordingly, we envision this platform as a promising approach for the systematic construction of conditional loss‐of‐function mutants. As proof of principle, we used this system to direct nuclear export of the essential heat shock transcription factor Hsf1p, thereby mimicking the cell‐cycle arrest phenotype of an hsf1 temperature‐sensitive mutant. Our drug‐induced localization platform also provides a method by which protein localization can be uncoupled from endogenous cell signalling events, addressing the necessity or sufficiency of a given localization shift for a particular cell process. To illustrate, we directed the nuclear import of the calcineurin‐dependent transcription factor Crz1p in the absence of native stimuli; this analysis directly substantiates that nuclear translocation of this protein is insufficient for its transcriptional activity. In total, this technology represents a powerful method for the generation of conditional alleles and directed mislocalization studies in yeast, with potential applicability on a genome‐wide scale. Copyright © 2008 John Wiley & Sons, Ltd." @default.
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• W2007580201 date "2008-07-30" @default.
• W2007580201 modified "2023-10-16" @default.
• W2007580201 title "A small molecule‐directed approach to control protein localization and function" @default.
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• W2007580201 doi "https://doi.org/10.1002/yea.1610" @default.
• W2007580201 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18668531" @default.
• W2007580201 hasPublicationYear "2008" @default.
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