Cytosolic Heat Shock Protein 90 in Plant Hormone and Environmental Stress Response

  • Kenji YamadaEmail author
  • Etsuko Watanabe
Part of the Heat Shock Proteins book series (HESP, volume 17)


From recent findings, it was revealed that cytosolic heat shock protein (HSP) 90 plays important roles in plant signal transduction during hormone sensing and environmental stress response. The various types of signaling proteins are identified as substrate for cytosolic HSP90 in plants; auxin receptor complex, auxin transporters, jasmonate receptor complex, brassinosteroid receptor complex, brassinosteroid-related transcription factors, heat shock transcription factors, receptors for pathogen infection, and components for circadian system. From the overview of these HSP90 substrates, cytosolic HSP90 works essentially in terms of sensing by receptor and output by transcription. It is also obvious that HSP90 facilitates SCF-type ubiquitin ligase complexes (e.g., auxin and jasmonate receptors) together with co-chaperone SGT1 in plants. This implies that cytosolic HSP90 regulates various SCF-type ubiquitin ligase complexes in other plant signaling systems. This chapter reviews recent advances in our understandings of cytosolic HSP90 function in plant hormones and environmental stress signaling.


Auxin Environmental stress Heat shock HSP90 Plant hormone Receptor 



auxin signaling F-box


auxin response factor


BRI1-associated receptor kinase 1


bin1-EMS-suppressor 1




brassinosteroid insensitive 1


brassinazole resistant 1


carboxyl terminus of Hsc70-interacting protein


coronatine insensitive 1


EIN3 binding F-box protein


FKBP-associated NAC


FK506-binding protein


gibberellic acid


gibberellin insensitive dwarf


heat shock transcription factor


heat shock protein


indole-3-acetic acid


jasmonic acid


light oxygen voltage


nucleotide binding leucine-rich repeat receptor


pasticcino 1




protein phosphatase 2A


peptidyl-prolyl cis/trans isomerases


Skp, Cullin, F-box-containing


suppressor of npr1 constitutive 1


transport inhibitor response 1


twisted dwarf





This work was supported in part by the National Science Center (UMO-2016/23/B/NZ1/01847), institutional support from Małopolska Centre of Biotechnology, Jagiellonian University.


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© Springer Nature Switzerland AG 2019

Authors and Affiliations

  1. 1.Małopolska Centre of BiotechnologyJagiellonian UniversityKrakówPoland
  2. 2.Department of Pathophysiology and MetabolismKawasaki Medical SchoolKurashikiJapan

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