HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in
            <i>Arabidopsis</i>

Takahashi, Akira; Casais, Catarina; Ichimura, Kazuya; Shirasu, Ken

doi:10.1073/pnas.2033934100

Cited by 442 publications

(446 citation statements)

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“…Pharmacological and genetic evidence supports the view that HSP90s also play a critical part in disease resistance mediated by another Arabidopsis NB-LRR protein, RPS2, upon recognition of its corresponding P. syringae effector, AvrRpt2 [8]. Either treatment with the HSP90 inhibitor geldanamycin or null mutation of AtHSP90.1 impaired an efficient resistance response to P. syringae expressing avrRpt2 and had weak effects on RPM1-dependent immunity.…”

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confidence: 74%

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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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confidence: 74%

“…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%

Plant Immunity: The Origami of Receptor Activation

Schulze-Lefert¹

2004

Current Biology

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“…However, several pieces of evidence might provide some clues to this question. Takahashi et al (2003) and HvHSP90 co-immuno-precipitated with HvSGT1 in barley plants [98]. The HSP90 proteins are members of the heat shock protein superfamily that are implicated in protein complex maturation, in the activation of innate immune system, and in regulating the activity of many signal transduction proteins [99][100][101].…”

Section: U-box-type E3 Ligases Are Newly Identified Members Of the Ubmentioning

confidence: 99%

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

et al. 2006

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Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.

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“…The function of these proteins in disease resistance responses have been extensively investigated previously using mutant analyses Chandra-Shekara et al, 2004;Hubert el al., 2003;Lu et al, 2003;Shirasu et al, 1999;Takahashi et al, 2003) and by virus induced gene silencing (VIGS) analyses in several plant species (Bhattarai et al, 2007;de la Fuente van Bentem et al, 2005;Leister et al, 2005;Liu et al, 2004;Scofield et al, 2005). The data from these studies revealed differing specificities for these proteins in diverse NB-LRR-mediated resistance responses.…”

Section: Discussionmentioning

confidence: 99%

“…For instance, it has been shown in Arabidopsis that RAR1 and HSP90, but not SGT1, are required for RPM1-, RPS2-, and RPS4-mediated immune responses Hubert et al, 2003;Takahashi et al, 2003). Similarly, RPP2-mediated resistance requires SGT1 but not RAR1.…”

Section: Discussionmentioning

confidence: 99%

Differential Requirement of Oryza sativa RAR1 in Immune Receptor-Mediated Resistance of Rice to Magnaporthe oryzae

Song

Kim

Han

et al. 2013

Molecules and Cells

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The required for Mla12 resistance (RAR1) protein is essential for the plant immune response. In rice, a model monocot species, the function of Oryza sativa RAR1 (OsRAR1) has been little explored. In our current study, we characterized the response of a rice osrar1 T-DNA insertion mutant to infection by Magnaporthe oryzae, the causal agent of rice blast disease. osrar1 mutants displayed reduced resistance compared with wild type rice when inoculated with the normally virulent M. oryzae isolate PO6-6, indicating that OsRAR1 is required for an immune response to this pathogen. We also investigated the function of Os-RAR1 in the resistance mechanism mediated by the immune receptor genes Pib and Pi5 that encode nucleotide binding-leucine rich repeat (NB-LRR) proteins. We inoculated progeny from Pib/osrar1 and Pi5/osrar1 heterozygous plants with the avirulent M. oryzae isolates, race 007 and PO6-6, respectively. We found that only Pib-mediated resistance was compromised by the osrar1 mutation and that the introduction of the OsRAR1 cDNA into Pib/osrar1 rescued Pib-mediated resistance. These results indicate that OsRAR1 is required for Pib-mediated resistance but not Pi5-mediated resistance to M. oryzae.

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HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis

Cited by 442 publications

References 43 publications

Plant Immunity: The Origami of Receptor Activation

Plant Immunity: The Origami of Receptor Activation

Ubiquitination-mediated protein degradation and modification: an emerging theme in plant-microbe interactions

Differential Requirement of Oryza sativa RAR1 in Immune Receptor-Mediated Resistance of Rice to Magnaporthe oryzae

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