After cellular damage caused by wounding or pathogens,Arabidopsis thaliana endogenous elicitor peptides(Peps)are released into the apoplast,enhancing innate immunity by directly binding to the membrane-localized leuci...After cellular damage caused by wounding or pathogens,Arabidopsis thaliana endogenous elicitor peptides(Peps)are released into the apoplast,enhancing innate immunity by directly binding to the membrane-localized leucine-rich repeat receptor kinase PEP RECEPTOR1(PEPR1).Ligand binding induces PEPR1 heterodimerization with the co-receptor BRASSINOSTEROID INSENSITIVE1-ASSOCIATED KINASE1(BAK1),followed by PEPR1internalization,both essential for a subset of Pep1-induced responses.However,the role of BAK1 in Pep1-triggered PEPR1 endocytosis remains unclear.Here,we show that the ligandinduced PEPR1 endocytosis depends on its kinase activity and requires BAK1 C-terminal tail phosphorylation,which is equally indispensable for immune signaling and BAK1 internalization.Using a GFP insertional mutagenesis approach,we generated a partially functional GFP-tagged BAK1 to demonstrate that,following Pep1 elicitation,BAK1 and PEPR1 are endocytosed together with similar dynamics.Our findings identify the BAK1 function as a prerequisite for PEPR1 internalization.展开更多
基金supported by special research funding from the Flemish Governmentfunding from the Student Program-Graduate Studies Plan Program from the Coordination for the Improvement of Higher Education Personnel(Brazil)for a joint doctorate fellowship at Ghent University and University of Sao Paulo to F.A.O.-.M.+8 种基金the European Union's Horizon 2020 research and innovation program under the Marie Sklodowska-Curie grant agreement(No.101023079‘ENDOLOGISTIC’)to S.Y.P.E.W.Latin American Fellows Program to F.A.O.-.M.the National Science Foundation(NSF)(MCB-1906060)to P.H.NSF(IOS-2049642)to L.S.the China Scholarship Council for a predoctoral fellowship(201706350153)a UGent BOF doctoral mandate(01CD7122)to X.X.the Research Foundation-Flanders(G003720N)to E.R.funded by Ghent University,FWOthe Flemish Government-department EWI。
文摘After cellular damage caused by wounding or pathogens,Arabidopsis thaliana endogenous elicitor peptides(Peps)are released into the apoplast,enhancing innate immunity by directly binding to the membrane-localized leucine-rich repeat receptor kinase PEP RECEPTOR1(PEPR1).Ligand binding induces PEPR1 heterodimerization with the co-receptor BRASSINOSTEROID INSENSITIVE1-ASSOCIATED KINASE1(BAK1),followed by PEPR1internalization,both essential for a subset of Pep1-induced responses.However,the role of BAK1 in Pep1-triggered PEPR1 endocytosis remains unclear.Here,we show that the ligandinduced PEPR1 endocytosis depends on its kinase activity and requires BAK1 C-terminal tail phosphorylation,which is equally indispensable for immune signaling and BAK1 internalization.Using a GFP insertional mutagenesis approach,we generated a partially functional GFP-tagged BAK1 to demonstrate that,following Pep1 elicitation,BAK1 and PEPR1 are endocytosed together with similar dynamics.Our findings identify the BAK1 function as a prerequisite for PEPR1 internalization.
