HSP90 stabilizes auxin receptor TIR1 and ensures plasticity of auxin responses

Plant Signaling & Behavior
Etsuko WatanabeKenji Yamada

Abstract

Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that facilitates the maturation of target proteins. Here, we report that the auxin receptor TIR1 is a target of cytosolic HSP90 and that HSP90 and TIR1 form a complex. Inhibition of HSP90 compromised the nuclear localization of TIR1, and abrogated plant responses to the hormone auxin. Our findings suggest that HSP90 positively regulates auxin receptor function. We also propose that HSP90 buffers or hides phenotypic variations in animals and plants by masking mutations in some of its target proteins. Support for this proposal comes from the tir1-1 mutant of Arabidopsis, which showed a root growth defect that was only seen after inhibition of HSP90. We have developed a model in which cytosolic HSP90 works like a capacitor for auxin-related phenotypic variation via regulation of the auxin receptor in response to environmentally and genetically induced perturbations.

References

Dec 9, 1998·Nature·S L Rutherford, S Lindquist
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Jun 7, 2002·Nature·Christine QueitschSusan Lindquist
Dec 12, 2002·Cellular and Molecular Life Sciences : CMLS·D Picard
Sep 25, 2003·Proceedings of the National Academy of Sciences of the United States of America·Akira TakahashiKen Shirasu
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Jun 10, 2010·Nature Reviews. Molecular Cell Biology·Mikko TaipaleSusan Lindquist
Nov 7, 2016·Plant & Cell Physiology·Etsuko WatanabeKenji Yamada

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Citations

Mar 12, 2019·Journal of Experimental Botany·Martin Kubeš, Richard Napier
Jul 10, 2019·Scientific Reports·Stefano D'AlessandroMaria Ruzzene
Aug 14, 2018·Plant Cell Reports·Jianhua XiangJieming Wang
Jun 13, 2018·International Journal of Molecular Sciences·Hayoung SongYoonkang Hur

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BETA
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