ScFKBP12 bridges rapamycin and AtTOR in Arabidopsis

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DOIResolve DOI: http://doi.org/10.4161/psb.26115
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TypeArticle
Journal titlePlant Signaling & Behavior
ISSN1559-2316
Volume8
Issue11
Pagese26115:1e26115:4; # of pages: 4
Subjectyeast FKBP12; rapamycin; FK506; Arabidopsis growth
AbstractFKBP12 encodes a prolyl isomerase and highly conserved in eukaryotic species. in yeasts and animals, FKBP12 can interact with rapamycin and FK506 to form rapamycin-FKBP12 and FK506-FKBP12 complex, respectively. in higher plants, FKBP12 protein lost its function to bind rapamycin and FK506. Early studies showed that yeast and human FKBP12 protein can restore the rapamycin sensitivity in Arabidopsis, but the used concentration is 100–1000 folds higher than that in yeast and animals. high concentration of drugs would increase the cost and cause the potential secondary effects on plant growth and development. here we further discovered that BP12 plants generated in our previous study are hypersensitive to rapamycin at the concentration as low as that is effective in yeast and animals. it is surprising to observe that Wt and BP12 plants are not sensitive to FK506 in normal growth condition. these findings advance the current understanding of rapamycin-tor signaling in plants.
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LanguageEnglish
Peer reviewedYes
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NRC number55932
NPARC number21271006
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Record identifiere5e0add2-81ce-4ab2-b292-daec9df6f17d
Record created2014-03-11
Record modified2016-05-09
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