Plant immunity is controlled by both positive regulators such as PBS3 and EDS1 and negative regulators such as NPR3 and NPR4.However,the relationships among these important immune regulators remain elusive.In this stu...Plant immunity is controlled by both positive regulators such as PBS3 and EDS1 and negative regulators such as NPR3 and NPR4.However,the relationships among these important immune regulators remain elusive.In this study,we found that PBS3 interacts with EDS1 in both the cytoplasm and the nucleus,and is required for EDS1 protein accumulation?NPR3 and NPR4,which function as salicylic acid receptors and adaptors of Cullin3-based E3 ligase,interact with and mediate the degradation of EDS1 via the 26S proteasome.We further discovered that PBS3 inhibits the polyubiquitination and subsequent degradation of EDS1 by reducing the association of EDS1 with the Cullin3 adaptors NPR3 and NPR4.Furthermore,we showed that PBS3 and EDS1 also contribute to PAMP-triggered immunity in addition to effector-triggered immunity.Collectively,our study reveals a novel mechanism by which plants fine-tune defense resporises by inhibiting the degradation of a positive player in plant immunity.展开更多
Poly(ADP-ribosyl)ation(PARylation)is a posttranslational modification reversibly catalyzed by poly(ADP-ribose)polymerases(PARPs)and poly(ADP-ribose)glycohydrolases(PARGs)and plays a key role in multi-ple cellular proc...Poly(ADP-ribosyl)ation(PARylation)is a posttranslational modification reversibly catalyzed by poly(ADP-ribose)polymerases(PARPs)and poly(ADP-ribose)glycohydrolases(PARGs)and plays a key role in multi-ple cellular processes.The molecular mechanisms by which PARylation regulates innate immunity remain largely unknown in eukaryotes.Here we show that Arabidopsis UBC13A and UBC13B,the major drivers of lysine 63(K63)-linked polyubiquitination,directly interact with PARPs/PARGs.Activation of pathogen-associated molecular pattern(PAMP)-triggered immunity promotes these interactions and enhances PARylation of UBC13.Both parp1 parp2 and ubc13a ubc13b mutants are compromised in immune responses with increased accumulation of total pathogenesis-related(PR)proteins but decreased accu-mulation of secreted PR proteins.Protein disulfide-isomerases(PDIs),essential components of endo-plasmic reticulum quality control(ERQC)that ensure proper folding and maturation of proteins destined for secretion,complex with PARPs/PARGs and are PARylated upon PAMP perception.Significantly,PARylation of UBC13 regulates K63-linked ubiquitination of PDIs,which may further promote their disulfide isomerase activities for correct protein folding and subsequent secretion.Taken together,these results indicate that plant immunity is coordinately regulated by PARylation and K63-linked ubiquitination.展开更多
Plant nucleotide-binding leucine-rich repeat(NLR)receptors mediate immune responses by directly or indirectly sensing pathogen-derived effectors.Despite significant advances in the understanding of NLR-mediated immuni...Plant nucleotide-binding leucine-rich repeat(NLR)receptors mediate immune responses by directly or indirectly sensing pathogen-derived effectors.Despite significant advances in the understanding of NLR-mediated immunity,the mechanisms by which pathogens evolve to suppress NLR activation triggered by cognate effectors and gain virulence remain largely unknown.The agronomically important immune receptor RB recognizes the ubiquitous and highly conserved IPI-O RXLR family members(e.g.,IPI-O1)from Phytophthora infestans,and this process is suppressed by the rarely present and homologous effector IPIO4.Here,we report that self-association of RB via the coiled-coil(CC)domain is required for RB activation and is differentially affected by avirulence and virulence effectors.IPI-O1 moderately reduces the self-association of RB CC,potentially leading to changes in the conformation and equilibrium of RB,whereas IPIO4 dramatically impairs CC self-association to prevent RB activation.We also found that IPI-O1 associates with itself,whereas IPI-O4 does not.Notably,IPI-O4 interacts with IPI-O1 and disrupts its self-association,therefore probably blocking its avirulence function.Furthermore,IPI-O4 enhances the interaction between RB CC and IPI-O1,possibly sequestering RB and IPI-O1 and subsequently blocking their interactions with signaling components.Taken together,these findings considerably extend our understanding of the underlying mechanisms by which emerging virulent pathogens suppress the NLR-mediated recognition of cognate effectors.展开更多
基金the National Natural Science Foundation of China(31701863)the University of South Carolina Office of Research(ASPIRE-I TrackllB,13010E244)the Postdoctoral Workstation of Jiangsu Academy of Agricultural Sciences.
文摘Plant immunity is controlled by both positive regulators such as PBS3 and EDS1 and negative regulators such as NPR3 and NPR4.However,the relationships among these important immune regulators remain elusive.In this study,we found that PBS3 interacts with EDS1 in both the cytoplasm and the nucleus,and is required for EDS1 protein accumulation?NPR3 and NPR4,which function as salicylic acid receptors and adaptors of Cullin3-based E3 ligase,interact with and mediate the degradation of EDS1 via the 26S proteasome.We further discovered that PBS3 inhibits the polyubiquitination and subsequent degradation of EDS1 by reducing the association of EDS1 with the Cullin3 adaptors NPR3 and NPR4.Furthermore,we showed that PBS3 and EDS1 also contribute to PAMP-triggered immunity in addition to effector-triggered immunity.Collectively,our study reveals a novel mechanism by which plants fine-tune defense resporises by inhibiting the degradation of a positive player in plant immunity.
基金supported by a start-up fund from Texas A&M AgriLife Research to J.S.a grant from the National Science Foundation(IOS-1951094)to P.H.and J.S.
文摘Poly(ADP-ribosyl)ation(PARylation)is a posttranslational modification reversibly catalyzed by poly(ADP-ribose)polymerases(PARPs)and poly(ADP-ribose)glycohydrolases(PARGs)and plays a key role in multi-ple cellular processes.The molecular mechanisms by which PARylation regulates innate immunity remain largely unknown in eukaryotes.Here we show that Arabidopsis UBC13A and UBC13B,the major drivers of lysine 63(K63)-linked polyubiquitination,directly interact with PARPs/PARGs.Activation of pathogen-associated molecular pattern(PAMP)-triggered immunity promotes these interactions and enhances PARylation of UBC13.Both parp1 parp2 and ubc13a ubc13b mutants are compromised in immune responses with increased accumulation of total pathogenesis-related(PR)proteins but decreased accu-mulation of secreted PR proteins.Protein disulfide-isomerases(PDIs),essential components of endo-plasmic reticulum quality control(ERQC)that ensure proper folding and maturation of proteins destined for secretion,complex with PARPs/PARGs and are PARylated upon PAMP perception.Significantly,PARylation of UBC13 regulates K63-linked ubiquitination of PDIs,which may further promote their disulfide isomerase activities for correct protein folding and subsequent secretion.Taken together,these results indicate that plant immunity is coordinately regulated by PARylation and K63-linked ubiquitination.
基金This work was supported by a start-up fund from Texas A&M AgriLife Research and a Hatch Project from the USDA National Institute of Food and Agriculture to J.S.(TEX0-1-9675).
文摘Plant nucleotide-binding leucine-rich repeat(NLR)receptors mediate immune responses by directly or indirectly sensing pathogen-derived effectors.Despite significant advances in the understanding of NLR-mediated immunity,the mechanisms by which pathogens evolve to suppress NLR activation triggered by cognate effectors and gain virulence remain largely unknown.The agronomically important immune receptor RB recognizes the ubiquitous and highly conserved IPI-O RXLR family members(e.g.,IPI-O1)from Phytophthora infestans,and this process is suppressed by the rarely present and homologous effector IPIO4.Here,we report that self-association of RB via the coiled-coil(CC)domain is required for RB activation and is differentially affected by avirulence and virulence effectors.IPI-O1 moderately reduces the self-association of RB CC,potentially leading to changes in the conformation and equilibrium of RB,whereas IPIO4 dramatically impairs CC self-association to prevent RB activation.We also found that IPI-O1 associates with itself,whereas IPI-O4 does not.Notably,IPI-O4 interacts with IPI-O1 and disrupts its self-association,therefore probably blocking its avirulence function.Furthermore,IPI-O4 enhances the interaction between RB CC and IPI-O1,possibly sequestering RB and IPI-O1 and subsequently blocking their interactions with signaling components.Taken together,these findings considerably extend our understanding of the underlying mechanisms by which emerging virulent pathogens suppress the NLR-mediated recognition of cognate effectors.
