Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein

Hubert, David A.; Tornero, Pablo; Belkhadir, Youssef; Krishna, Priti; Takahashi, Akira; Shirasu, Ken; Dangl, Jeffery L.

doi:10.1093/emboj/cdg547

Cited by 356 publications

(401 citation statements)

References 60 publications

(123 reference statements)

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“…So far, genetic approaches have identified relatively few components required for R gene function in plants [5]. A highly conserved protein class, the heat-shock proteins, has now been added to the list and work on these proteins promises to provide fresh insights to the molecular mechanics of the pathogen recognition process [6][7][8][9].…”

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confidence: 99%

“…Hubert et al [7] used a genetic approach which revealed cytosolic HSP90s as critical components in immunity triggered by an NB-LRR type R protein. Rare specific mutations in one of four Arabidopsis genes encoding cytosolic HSP90 isoforms were identified in a large-scale conditional screen for mutants impaired in resistance triggered by the R protein RPM1 upon recognition of the Pseudomonas syringae effector AvrRpm1 [7].…”

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confidence: 99%

“…Rare specific mutations in one of four Arabidopsis genes encoding cytosolic HSP90 isoforms were identified in a large-scale conditional screen for mutants impaired in resistance triggered by the R protein RPM1 upon recognition of the Pseudomonas syringae effector AvrRpm1 [7]. Analysis of the recovered mutant alleles showed that all three were generated by single amino acid substitutions in the ATPase domain of HSP90.2, drastically reducing the steady-state levels of RPM1 in non-challenged plants but not interfering with the resistance reactions triggered by seven other tested R genes.…”

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“…Hubert et al [7] thus concluded that HSP90.2 has a role in folding RPM1 into a stable conformation or a signalling competent RPM1-containing complex. Preliminary evidence for the latter was obtained by co-immunoprecipitation experiments involving the Arabidopsis RIN4 protein.…”

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“…An indication that the former might be true is the observation that RPM1 steady-state levels are greatly decreased or undetectable in non-challenged rar1 or hsp90.2 mutant backgrounds [7,19]. The role of SGT1 in R protein function is likely to be different, because RX protein accumulation was impaired following NbHSP90 silencing but unaffected upon NbSGT1 silencing [9].…”

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Plant Immunity: The Origami of Receptor Activation

Schulze-Lefert¹

2004

Current Biology

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Mutations in plant cytosolicOne of the HSP90.2 substitutions is equivalent to that creating a mutant form of yeast HSP90 that lacks the ATPase activity required for client turnover, yet retains the ability to dimerize. Paradoxically, an insertion allele of AtHSP90.2, presumably a null mutation, had no discernible effect on RPM1 function. Furthermore, the Athsp90.2 mutant alleles with ATP binding site substitutions revealed a baroque genetic condition known as 'non-allelic non-complementation'. In such cases, F 1 heterozygous products of a cross between plants bearing two unlinked recessive mutations are phenotypically similar to either homozygous single mutant. In this particular case, F 1 plants containing wild-type and mutant alleles of both RPM1 and HSP90.2 were susceptible to P. syringae expressing avrRpm1.Non-allelic non-complementation provides clear evidence for dosage-sensitivity, and also suggests close physical associations -either direct physical interaction between RPM1 and HSP90.2 or an association in the same complex. Indeed, co-immunoprecipitation of RPM1 and HSP90 from plant extracts supported the conclusion that the proteins associate in vivo, although it remains to be shown whether the interaction is really direct and preferentially involves HSP90.2 and/or any of the other three closely related cytosolic HSP90 isoforms. One way of rationalizing the findings invokes functional redundancy in the HSP90 family, which could prevent inactivation of RPM1 in the Athsp90.2 null mutant, whereas mutations of the HSP90.2 ATPase domain might prohibit functional redundancy by causing persistent, but non-productive, client binding.In this scenario, non-productive binding might force incompletely folded RPM1 to enter a default degradation pathway. Hubert et al.[7] thus concluded that HSP90.2 has a role in folding RPM1 into a stable conformation or a signalling competent RPM1-containing complex. Preliminary evidence for the latter was obtained by co-immunoprecipitation experiments involving the Arabidopsis RIN4 protein. RIN4 is another component essential for RPM1 function and is known to interact directly with both RPM1 and the cognate Pseudomonas effector AvrRpm1 on the cytoplasmic face of plant plasma membranes [2]. In co-immunoprecipitation experiments, RIN4 did not appear to interact with HSP90, suggesting the existence of at least two pools of RPM1. This may also indicate that HSP90 acts transiently in the assembly of an RPM1-containing

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Plant Immunity: The Origami of Receptor Activation

Schulze-Lefert¹

2004

Current Biology

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HSP90 and co‐chaperones: a multitaskers’ view on plant hormone biology

Donato

Geisler

2019

FEBS Letters

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In order to survive under ever‐changing conditions plants must be able to adaptively respond to their environment. Plant hormones and the signaling cross‐talk among them play a key role in integrating external and internal cues, enabling the plants to acclimate accordingly. HSP90 and several of its co‐chaperones are known as pleiotropic factors involved in the signaling pathways of multiple stress responses, including temperature, drought, and pathogen infection. Recently, hormone receptor components for auxin and jasmonic acid, respectively, have been identified as clients of the HSP90 chaperone system, suggesting a direct HSP90‐dependent link to hormone signaling. In this review, we give an overview of the multiple roles of HSP90 and its co‐chaperones in plant hormone biology and discuss the largely unexplored targets for signal integration that the activity of these apparent multitaskers may suggest.

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Plant Abiotic Stress

Jenks

Hasegawa

2005

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of CBF gene expression in response to low temperature 4.2.4.1 DNA regulatory elements controlling CBF expression 4.2.4.2 Proteins with positive roles in CBF expression 4.2.4.3 Proteins with negative roles in CBF expression 4.2.4.4 Other potential CBF regulatory proteins 4.2.4.5 Light and circadian rhythms 4.2.4.6 Role of calcium 4.2.4.7 Role of ABA 4.3 Conservation of the CBF cold-response pathway 4.3.1 Brassica napus 4.3.2 Tomato 4.3.3 Rice 4.4 Concluding remarks 5 Plant responses to high temperature JANE LARKINDALE, MICHAEL MISHKIND and ELIZABETH VIERLING 5.1 Introduction 5.2 Physiological responses to high temperature 5.2.1 High temperature limits to optimal plant performance 5.2.2 Heat sensitivity of photosynthesis 5.2.3 Heat sensitivity of reproduction 5.3 Cellular acquired thermotolerance 5.4 Heat shock proteins/molecular chaperones 5.4.1 Hsp100/ClpB 5.4.2 Hsp90 5.4.3 Hsp70/DnaK 5.4.4 Hsp60/GroE 5.4.5 The sHSP family of proteins 5.5 Other components of the response to heat 5.5.1 Antioxidant production 5.5.2 Other heat-stress regulated genes 5.5.3 Other heat-protective responses 5.5.4 Mutants defective in heat tolerance 5.5.5 Transgenic plants with altered heat tolerance CONTENTS vii 5.6 Signaling pathways involved in response to heat 5.6.1 Heat shock transcription factors 5.6.2 Other signaling pathways 5.6.3 Abscisic acid 5.6.4 Salicylic acid

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Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein

Cited by 356 publications

References 60 publications

Plant Immunity: The Origami of Receptor Activation

Plant Immunity: The Origami of Receptor Activation

HSP90 and co‐chaperones: a multitaskers’ view on plant hormone biology

Plant Abiotic Stress

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