VPEγ Exhibits a Caspase-like Activity that Contributes to Defense against Pathogens

Rojo, Enrique; Martı́n, Raquel; Carter, Clay; Zouhar, Jan; Pan, Songqin; Plotnikova, Julia M.; Jin, Hailing; Paneque, Manuel; Sánchez‐Serrano, José J.; Baker, Barbara; Ausubel, Frederick M.; Raikhel, Natasha V.

doi:10.1016/j.cub.2004.09.056

Cited by 238 publications

(200 citation statements)

References 35 publications

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“…Furthermore, VPE mutants were also markedly more susceptible to these pathogens. When VPE was overexpressed, cell death markers (e.g., ion leakage) were observed (Rojo et al, 2004). Thus, although strictly speaking, bona fide caspases are not present in plant genomes, caspase-1-like activities are found in plants and in several cases contribute to the outcome of several plant microbe interactions.…”

Section: Discussionmentioning

confidence: 99%

Aspartyl Protease-Mediated Cleavage of BAG6 Is Necessary for Autophagy and Fungal Resistance in Plants

et al. 2016

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The Bcl-2-associated athanogene (BAG) family is an evolutionarily conserved group of cochaperones that modulate numerous cellular processes. Previously we found that Arabidopsis thaliana BAG6 is required for basal immunity against the fungal phytopathogen Botrytis cinerea. However, the mechanisms by which BAG6 controls immunity are obscure. Here, we address this important question by determining the molecular mechanisms responsible for BAG6-mediated basal resistance. We show that Arabidopsis BAG6 is cleaved in vivo in a caspase-1-like-dependent manner and via a combination of pulldowns, mass spectrometry, yeast two-hybrid assays, and chemical genomics, we demonstrate that BAG6 interacts with a C2 GRAM domain protein (BAGP1) and an aspartyl protease (APCB1), both of which are required for BAG6 processing. Furthermore, fluorescence and transmission electron microscopy established that BAG6 cleavage triggers autophagy in the host that coincides with disease resistance. Targeted inactivation of BAGP1 or APCB1 results in the blocking of BAG6 processing and loss of resistance. Mutation of the cleavage site blocks cleavage and inhibits autophagy in plants; disease resistance is also compromised. Taken together, these results identify a mechanism that couples an aspartyl protease with a molecular cochaperone to trigger autophagy and plant defense, providing a key link between fungal recognition and the induction of cell death and resistance.

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Section: Discussionmentioning

confidence: 99%

Aspartyl Protease-Mediated Cleavage of BAG6 Is Necessary for Autophagy and Fungal Resistance in Plants

et al. 2016

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“…Several transgenic plant lines expressing exogenous cystatins were successfully produced over the last 15 years (e.g. Masoud et al, 1993;Benchekroun et al, 1995;Leplé et al, 1995;GutierrezCampos et al, 1999;Van der Vyver et al, 2003;Outchkourov et al, 2004), but recent studies reported pleiotropic effects of these proteins affecting major biological processes such as flowering, programmed cell death, tolerance to biotic stresses, and defense protein induction (Gutierrez-Campos et al, 2001;Belenghi et al, 2003;Van der Vyver et al, 2003;Rojo et al, 2004;Vaillancourt, 2005). Little is still known about the exact regulatory functions of Cys proteases in plant cells, but their obvious importance at the genome level (Beers et al, 2004) and their broad distribution in plant tissues and cells (Grudkowska and Zagdanska, 2004;Schaller, 2004) suggest a significant role for these enzymes in various cellular and developmental processes.…”

Section: Discussionmentioning

confidence: 99%

Tailoring the Specificity of a Plant Cystatin toward Herbivorous Insect Digestive Cysteine Proteases by Single Mutations at Positively Selected Amino Acid Sites

et al. 2008

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Plant cystatins, similar to other defense proteins, include hypervariable, positively selected amino acid sites presumably impacting their biological activity. Using 29 single mutants of the eighth domain of tomato (Solanum lycopersicum) multicystatin, SlCYS8, we assessed here the potential of site-directed mutagenesis at positively selected amino acid sites to generate cystatin variants with improved inhibitory potency and specificity toward herbivorous insect digestive cysteine (Cys) proteases. Compared to SlCYS8, several mutants (22 out of 29) exhibited either improved or lowered potency against different model Cys proteases, strongly suggesting the potential of positively selected amino acids as target sites to modulate the inhibitory specificity of the cystatin toward Cys proteases of agronomic significance. Accordingly, mutations at positively selected sites strongly influenced the inhibitory potency of SlCYS8 against digestive Cys proteases of the insect herbivore Colorado potato beetle (Leptinotarsa decemlineata). In particular, several variants exhibited improved potency against both cystatin-sensitive and cystatininsensitive digestive Cys proteases of this insect. Of these, some variants also showed weaker activity against leaf Cys proteases of the host plant (potato [Solanum tuberosum]) and against a major digestive Cys protease of the two-spotted stinkbug Perillus bioculatus, an insect predator of Colorado potato beetle showing potential for biological control. Overall, these observations suggest the usefulness of site-directed mutagenesis at positively selected amino acid sites for the engineering of recombinant cystatins with both improved inhibitory potency toward the digestive proteases of target herbivores and weaker potency against nontarget Cys proteases in the host plant or the environment.

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“…[88][89][90][91] The vacuolar processing enzyme VPE in Nicotiana benthamiana and its homolog VPEgamma in Arabidopsis have caspase-1-like activity during HR. 89,91 Additionally, vacuolar fusion to the plasma membrane mediated by a caspase-3-like activity of PBA1, a plant proteasome subunit, was suggested to be a functionally relevant early event in NLR-mediated HR. 88 More than a decade ago, two new families of caspase-like proteins, metacaspases and paracaspases, were identified in silico 92 (Figure 4b).…”

Section: The Type I Metacaspase Regulatory Module In Hrmentioning

confidence: 99%

Programmed cell death in the plant immune system

2011

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Cell death has a central role in innate immune responses in both plants and animals. Besides sharing striking convergences and similarities in the overall evolutionary organization of their innate immune systems, both plants and animals can respond to infection and pathogen recognition with programmed cell death. The fact that plant and animal pathogens have evolved strategies to subvert specific cell death modalities emphasizes the essential role of cell death during immune responses. The hypersensitive response (HR) cell death in plants displays morphological features, molecular architectures and mechanisms reminiscent of different inflammatory cell death types in animals (pyroptosis and necroptosis). In this review, we describe the molecular pathways leading to cell death during innate immune responses. Additionally, we present recently discovered caspase and caspase-like networks regulating cell death that have revealed fascinating analogies between cell death control across both kingdoms.

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VPEγ Exhibits a Caspase-like Activity that Contributes to Defense against Pathogens

Abstract: We conclude that VPEgamma is a caspase-like enzyme that has been recruited in plants to regulate vacuole-mediated cell dismantling during cell death, a process that has significant influence in the outcome of a diverse set of plant-pathogen interactions.

Cited by 238 publications

References 35 publications

Aspartyl Protease-Mediated Cleavage of BAG6 Is Necessary for Autophagy and Fungal Resistance in Plants

Aspartyl Protease-Mediated Cleavage of BAG6 Is Necessary for Autophagy and Fungal Resistance in Plants

Tailoring the Specificity of a Plant Cystatin toward Herbivorous Insect Digestive Cysteine Proteases by Single Mutations at Positively Selected Amino Acid Sites

Programmed cell death in the plant immune system

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