Tomato FK506 Binding Protein 12KD (FKBP12) mediates the interaction between rapamycin and Target of Rapamycin (TOR)

Target of Rapamycin (TOR) signaling is an important regulator in multiple organisms including yeast, plants and animals. However, the TOR signaling in plants is much less understood as compared to that in yeast and animals. TOR kinase can be efficiently suppressed by rapamycin in the presence of fun...

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Main Authors: Fangjie Xiong, Pan Dong, Mei Liu, Gengxin Xie, Kai Wang, Fengping Zhuo, Li Feng, Lu Yang, Zhengguo Li, Maozhi Ren
Format: Article
Language:English
Published: Frontiers Media S.A. 2016-11-01
Series:Frontiers in Plant Science
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fpls.2016.01746/full
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author Fangjie Xiong
Pan Dong
Mei Liu
Gengxin Xie
Kai Wang
Fengping Zhuo
Li Feng
Lu Yang
Zhengguo Li
Maozhi Ren
author_facet Fangjie Xiong
Pan Dong
Mei Liu
Gengxin Xie
Kai Wang
Fengping Zhuo
Li Feng
Lu Yang
Zhengguo Li
Maozhi Ren
author_sort Fangjie Xiong
collection DOAJ
description Target of Rapamycin (TOR) signaling is an important regulator in multiple organisms including yeast, plants and animals. However, the TOR signaling in plants is much less understood as compared to that in yeast and animals. TOR kinase can be efficiently suppressed by rapamycin in the presence of functional FK506 Binding Protein 12KD (FKBP12) in yeast and animals. In most examined higher plants rapamycin fails to inhibit TOR kinase due to the non-functional FKBP12. Here we find that tomato plants showed obvious growth inhibition when treated with rapamycin and the inhibitory phenotype is similar to suppression of TOR causing by active-site TOR inhibitors (asTORis) such as KU63794, AZD8055 and Torin1. The chemical genetic assays using TOR inhibitors and heterologous expressing SlFKBP12 in Arabidopsis indicated that the TOR signaling is functional in tomato. The protein gel shifting and TOR inhibitors combination assays showed that SlFKBP12 can mediate the interaction between rapamycin and TOR. Furthermore, comparative expression profiling analysis between treatments with rapamycin and KU63794 identified highly overlapped Differentially Expressed Genes (DEGs) which are involved in many anabolic and catabolic processes, such as photosynthesis, cell wall restructuring, and senescence in tomato. These observations suggest that SlFFBP12 is functional in tomato. The results provided basic information of TOR signaling in tomato, and also some new insights into how TOR controls plant growth and development through reprogramming the transcription profiles
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spelling doaj.art-409181f261d54b319d683abe697addb32022-12-21T19:55:03ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2016-11-01710.3389/fpls.2016.01746216460Tomato FK506 Binding Protein 12KD (FKBP12) mediates the interaction between rapamycin and Target of Rapamycin (TOR)Fangjie Xiong0Pan Dong1Mei Liu2Gengxin Xie3Kai Wang4Fengping Zhuo5Li Feng6Lu Yang7Zhengguo Li8Maozhi Ren9Chongqing UniversityChongqing UniversityChongqing UniversityChongqing UniversityChongqing UniversityChongqing UniversityChongqing UniversityChongqing UniversityChongqing UniversityChongqing UniversityTarget of Rapamycin (TOR) signaling is an important regulator in multiple organisms including yeast, plants and animals. However, the TOR signaling in plants is much less understood as compared to that in yeast and animals. TOR kinase can be efficiently suppressed by rapamycin in the presence of functional FK506 Binding Protein 12KD (FKBP12) in yeast and animals. In most examined higher plants rapamycin fails to inhibit TOR kinase due to the non-functional FKBP12. Here we find that tomato plants showed obvious growth inhibition when treated with rapamycin and the inhibitory phenotype is similar to suppression of TOR causing by active-site TOR inhibitors (asTORis) such as KU63794, AZD8055 and Torin1. The chemical genetic assays using TOR inhibitors and heterologous expressing SlFKBP12 in Arabidopsis indicated that the TOR signaling is functional in tomato. The protein gel shifting and TOR inhibitors combination assays showed that SlFKBP12 can mediate the interaction between rapamycin and TOR. Furthermore, comparative expression profiling analysis between treatments with rapamycin and KU63794 identified highly overlapped Differentially Expressed Genes (DEGs) which are involved in many anabolic and catabolic processes, such as photosynthesis, cell wall restructuring, and senescence in tomato. These observations suggest that SlFFBP12 is functional in tomato. The results provided basic information of TOR signaling in tomato, and also some new insights into how TOR controls plant growth and development through reprogramming the transcription profileshttp://journal.frontiersin.org/Journal/10.3389/fpls.2016.01746/fullTomatorapamycingene expression profileTarget of rapamycinKU63794SlFKBP12
spellingShingle Fangjie Xiong
Pan Dong
Mei Liu
Gengxin Xie
Kai Wang
Fengping Zhuo
Li Feng
Lu Yang
Zhengguo Li
Maozhi Ren
Tomato FK506 Binding Protein 12KD (FKBP12) mediates the interaction between rapamycin and Target of Rapamycin (TOR)
Frontiers in Plant Science
Tomato
rapamycin
gene expression profile
Target of rapamycin
KU63794
SlFKBP12
title Tomato FK506 Binding Protein 12KD (FKBP12) mediates the interaction between rapamycin and Target of Rapamycin (TOR)
title_full Tomato FK506 Binding Protein 12KD (FKBP12) mediates the interaction between rapamycin and Target of Rapamycin (TOR)
title_fullStr Tomato FK506 Binding Protein 12KD (FKBP12) mediates the interaction between rapamycin and Target of Rapamycin (TOR)
title_full_unstemmed Tomato FK506 Binding Protein 12KD (FKBP12) mediates the interaction between rapamycin and Target of Rapamycin (TOR)
title_short Tomato FK506 Binding Protein 12KD (FKBP12) mediates the interaction between rapamycin and Target of Rapamycin (TOR)
title_sort tomato fk506 binding protein 12kd fkbp12 mediates the interaction between rapamycin and target of rapamycin tor
topic Tomato
rapamycin
gene expression profile
Target of rapamycin
KU63794
SlFKBP12
url http://journal.frontiersin.org/Journal/10.3389/fpls.2016.01746/full
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