In this paper,we investigate some new interesting solution structures of the(2+1)-dimensional bidirectional Sawada–Kotera(bSK)equation.We obtain soliton molecules by introducing velocity resonance.On the basis of sol...In this paper,we investigate some new interesting solution structures of the(2+1)-dimensional bidirectional Sawada–Kotera(bSK)equation.We obtain soliton molecules by introducing velocity resonance.On the basis of soliton molecules,asymmetric solitons are obtained by changing the distance between two solitons of molecules.Based on the N-soliton solutions,several novel types of mixed solutions are generated,which include the mixed breather-soliton molecule solution by the module resonance of the wave number and partial velocity resonance,the mixed lump-soliton molecule solution obtained by partial velocity resonance and partial long wave limits,and the mixed solutions composed of soliton molecules(asymmetric solitons),lump waves,and breather waves.Some plots are presented to clearly illustrate the dynamic features of these solutions.展开更多
Plants employ receptor-like kinases (RLKs)and receptor-like proteins for rapid recognition of invading pathogens,and RLKs then transmit signals to receptor-like cytoplasmic kinases (RLCKs)to activate immune responses....Plants employ receptor-like kinases (RLKs)and receptor-like proteins for rapid recognition of invading pathogens,and RLKs then transmit signals to receptor-like cytoplasmic kinases (RLCKs)to activate immune responses.RLKs are under fine regulation mediated by subcellular trafficking,which contributes to proper activation of plant immunity.In this study,we show that Arabidopsisthaliana RECEPTOR-LIKE KINASE 902 (RLK902)plays important roles in resistance to the bacterial pathogen Pseudomonas syringae, but not to the fungal powdery mildew pathogen Golovinomyces cichoracearum.RLK902 localizes at the plasma membrane and associates with ENHANCED DISEASE RESISTANCE 4 (EDR4),a protein involved in clathrin-mediated trafficking pathways.EDR4 and CLATHRIN HEAVY CHAIN 2 (CHC2)regulate the subcellular trafficking and accumulation of RLK902 protein.Furthermore,we found that RLKg02 directly associates with the RLCK BRASSINOSTEROID-SIGNALING KINASE1 (BSK1),a key component of plant immunity,but not with other members of the FLAGELLIN SENSING 2 immune complex.RLK902 phosphorylates BSK1,and its Ser-230 is a key phosphorylation site critical for RLK902-mediated defense signaling. Taken together,our data indicate that EDR4 regulates plant immunity by modulating the subcellular trafficking and protein accumulation of RLK902,and that RLK902 transmits immune signals by phosphorylating BSK1.展开更多
Growth and immunity are opposing processes that compete for cellular resources,and proper resource allocation is crucial for plant survival.BSK1 plays a key role in the regulation of both growth and immunity by associ...Growth and immunity are opposing processes that compete for cellular resources,and proper resource allocation is crucial for plant survival.BSK1 plays a key role in the regulation of both growth and immunity by associating with BRI1 and FLS2,respectively.However,it remains unclear how two antagonistic signals co-opt BSK1 to induce signal-specific activation.Here we show that the dynamic spatial reorganiization of BSK1 within the plasma membrane underlies the mechanism of signal-specific activation for growth or immunity.Resting BSK1 localizes to membrane rafts as complexes.Unlike BSK1-associated FLS2 and BRI1,flg22 or exogenous brassinosteroid(BR)treatment did not decrease BSK1 levels at the plasma membrane(PM)but rather induced BSK1 multimerization and dissociation from FLS2/BSK1 or BRI1/BSK1,respectively.Moreover,flg22-activated BSK1 translocated from membrane rafts to non-membrane-raft regions,whereas BR-activated BSK1 remained in membrane rafts.When applied together with flg22,BR suppressed various flg22-induced BSK1 activities such as BSK1 dissociation from FLS2/BSK1,BSK1 interaction with MAPKKK5,and BSK translocation together with MAPKKK5.Taken together,this study provides a unique insight into how the precise control of BSK1 spatiotemporal organization regulates the signaling specificity to balance plant growth and immunity.展开更多
Cell-surface-localized leucine-rich-repeat receptorlike kinases(LRR-RLKs)are crucial for plant immunity.Most LRR-RLKs that act as receptors directly recognize ligands via a large extracellular domain(ECD),whereas LRR-...Cell-surface-localized leucine-rich-repeat receptorlike kinases(LRR-RLKs)are crucial for plant immunity.Most LRR-RLKs that act as receptors directly recognize ligands via a large extracellular domain(ECD),whereas LRR-RLK that serve as regulators are relatively small and contain fewer LRRs.Here,we identified LRR-RLK regulators using high-throughput tobacco rattle virus(TRV)-based gene silencing in the model plant Nicotiana benthamiana.We used the cell-death phenotype caused by INF1,an oomycete elicitin that induces pattern-triggered immunity,as an indicator.By screening 33 small LRR-RLKs(≤6 LRRs)of unknown function,we identified ELICITIN INSENSITIVE RLK 1(NbEIR1)as a positive regulator of INF1-induced immunity and oomycete resistance.Nicotiana benthamiana mutants of eir1 generated by CRISPR/Cas9-editing showed significantly compromised immune responses to INF1 and were more vulnerable to the oomycete pathogen Phytophthora capsici.NbEIR1 associates with BRI1-ASSOCIATED RECEPTOR KINASE 1(NbBAK1)and a downstream component,BRASSINOSTEROIDSIGNALING KINASE 1(NbBSK1).NbBSK1 also contributes to INF1-induced defense and P.capsici resistance.Upon INF1 treatment,NbEIR1 was released from NbBAK1 and NbBSK1 in vivo.Moreover,the silencing of NbBSK1 compromised the association of NbEIR1 with NbBAK1.We also showed that NbEIR1 regulates flg22-induced immunity and associates with its receptor,FLAGELLIN SENSING 2(NbFLS2).Collectively,our results suggest that NbEIR1 is a novel regulatory element for BAK1-dependent immunity.NbBSK1-NbEIR1 association is required for maintaining the NbEIR1/NbBAK1 complex in the resting state.展开更多
近日,陕西交通职业技术学院举办国际交流合作项目签约仪式,该院院长杨云峰、德国BSK国际教育机构执行总裁凯尔·费德勒(Kai Arne Fielder)代表双方签字。签约仪式由该院副院长李吟龙主持。该院院长助理张小科和党政办、继续教育...近日,陕西交通职业技术学院举办国际交流合作项目签约仪式,该院院长杨云峰、德国BSK国际教育机构执行总裁凯尔·费德勒(Kai Arne Fielder)代表双方签字。签约仪式由该院副院长李吟龙主持。该院院长助理张小科和党政办、继续教育与国际交流学院、汽车工程学院、人事处有关负责人参加签约仪式。展开更多
基金supported by the National Natural Science Foundation of China(Nos.11775121 and 11435005)the Dean’s Research Fund 2017-18(FLASS/DRF/IRS-10)from the Education University of Hong Kongthe KC Wong Magna Fund at Ningbo University.
文摘In this paper,we investigate some new interesting solution structures of the(2+1)-dimensional bidirectional Sawada–Kotera(bSK)equation.We obtain soliton molecules by introducing velocity resonance.On the basis of soliton molecules,asymmetric solitons are obtained by changing the distance between two solitons of molecules.Based on the N-soliton solutions,several novel types of mixed solutions are generated,which include the mixed breather-soliton molecule solution by the module resonance of the wave number and partial velocity resonance,the mixed lump-soliton molecule solution obtained by partial velocity resonance and partial long wave limits,and the mixed solutions composed of soliton molecules(asymmetric solitons),lump waves,and breather waves.Some plots are presented to clearly illustrate the dynamic features of these solutions.
文摘Plants employ receptor-like kinases (RLKs)and receptor-like proteins for rapid recognition of invading pathogens,and RLKs then transmit signals to receptor-like cytoplasmic kinases (RLCKs)to activate immune responses.RLKs are under fine regulation mediated by subcellular trafficking,which contributes to proper activation of plant immunity.In this study,we show that Arabidopsisthaliana RECEPTOR-LIKE KINASE 902 (RLK902)plays important roles in resistance to the bacterial pathogen Pseudomonas syringae, but not to the fungal powdery mildew pathogen Golovinomyces cichoracearum.RLK902 localizes at the plasma membrane and associates with ENHANCED DISEASE RESISTANCE 4 (EDR4),a protein involved in clathrin-mediated trafficking pathways.EDR4 and CLATHRIN HEAVY CHAIN 2 (CHC2)regulate the subcellular trafficking and accumulation of RLK902 protein.Furthermore,we found that RLKg02 directly associates with the RLCK BRASSINOSTEROID-SIGNALING KINASE1 (BSK1),a key component of plant immunity,but not with other members of the FLAGELLIN SENSING 2 immune complex.RLK902 phosphorylates BSK1,and its Ser-230 is a key phosphorylation site critical for RLK902-mediated defense signaling. Taken together,our data indicate that EDR4 regulates plant immunity by modulating the subcellular trafficking and protein accumulation of RLK902,and that RLK902 transmits immune signals by phosphorylating BSK1.
基金This work was supported by the Program of Introducing Talents of Discipline to Universities(111 Project,B13007 to J.L.)the National Natural Science Foundation of China(32030010 and 31530084 to J.L.,31871424 to X.S.).
文摘Growth and immunity are opposing processes that compete for cellular resources,and proper resource allocation is crucial for plant survival.BSK1 plays a key role in the regulation of both growth and immunity by associating with BRI1 and FLS2,respectively.However,it remains unclear how two antagonistic signals co-opt BSK1 to induce signal-specific activation.Here we show that the dynamic spatial reorganiization of BSK1 within the plasma membrane underlies the mechanism of signal-specific activation for growth or immunity.Resting BSK1 localizes to membrane rafts as complexes.Unlike BSK1-associated FLS2 and BRI1,flg22 or exogenous brassinosteroid(BR)treatment did not decrease BSK1 levels at the plasma membrane(PM)but rather induced BSK1 multimerization and dissociation from FLS2/BSK1 or BRI1/BSK1,respectively.Moreover,flg22-activated BSK1 translocated from membrane rafts to non-membrane-raft regions,whereas BR-activated BSK1 remained in membrane rafts.When applied together with flg22,BR suppressed various flg22-induced BSK1 activities such as BSK1 dissociation from FLS2/BSK1,BSK1 interaction with MAPKKK5,and BSK translocation together with MAPKKK5.Taken together,this study provides a unique insight into how the precise control of BSK1 spatiotemporal organization regulates the signaling specificity to balance plant growth and immunity.
基金supported by the National Natural Science Foundation of China(32100155 and 32072507)the Natural Science Foundation of Jiangsu Province(BK20221000)+1 种基金the fellowship of China Postdoctoral Science Foundation(2021M701740)the Jiangsu Funding Program for Excellent Postdoctoral Talent(2022ZB343 and 2022ZB768)。
文摘Cell-surface-localized leucine-rich-repeat receptorlike kinases(LRR-RLKs)are crucial for plant immunity.Most LRR-RLKs that act as receptors directly recognize ligands via a large extracellular domain(ECD),whereas LRR-RLK that serve as regulators are relatively small and contain fewer LRRs.Here,we identified LRR-RLK regulators using high-throughput tobacco rattle virus(TRV)-based gene silencing in the model plant Nicotiana benthamiana.We used the cell-death phenotype caused by INF1,an oomycete elicitin that induces pattern-triggered immunity,as an indicator.By screening 33 small LRR-RLKs(≤6 LRRs)of unknown function,we identified ELICITIN INSENSITIVE RLK 1(NbEIR1)as a positive regulator of INF1-induced immunity and oomycete resistance.Nicotiana benthamiana mutants of eir1 generated by CRISPR/Cas9-editing showed significantly compromised immune responses to INF1 and were more vulnerable to the oomycete pathogen Phytophthora capsici.NbEIR1 associates with BRI1-ASSOCIATED RECEPTOR KINASE 1(NbBAK1)and a downstream component,BRASSINOSTEROIDSIGNALING KINASE 1(NbBSK1).NbBSK1 also contributes to INF1-induced defense and P.capsici resistance.Upon INF1 treatment,NbEIR1 was released from NbBAK1 and NbBSK1 in vivo.Moreover,the silencing of NbBSK1 compromised the association of NbEIR1 with NbBAK1.We also showed that NbEIR1 regulates flg22-induced immunity and associates with its receptor,FLAGELLIN SENSING 2(NbFLS2).Collectively,our results suggest that NbEIR1 is a novel regulatory element for BAK1-dependent immunity.NbBSK1-NbEIR1 association is required for maintaining the NbEIR1/NbBAK1 complex in the resting state.