DEK protein is an ubiquitous phosphorylated nuclear protein.Specific binding of DEK to DNA could change the topology of DNA and then affect the gene activity of the underlying DNA sequences.It is speculated that there...DEK protein is an ubiquitous phosphorylated nuclear protein.Specific binding of DEK to DNA could change the topology of DNA and then affect the gene activity of the underlying DNA sequences.It is speculated that there might be some potential relationship between the stress reaction of cells and DEK proteins.The phosphorylation status of DEK protein is altered during death-receptor-mediated cell apoptosis.Both phosphorylation and poly(ADP-ribosyl)ation could promote the release of DEK from apoptotic nuclei to extracellular environment,and in this case DEK becomes a potential autoantigen of some autoimmune diseases.The available evidence powerfully suggests that DEK protein is closely relevant to apoptosis.The overexpression of DEK protein has dual function in cell apoptosis,in terms of inhibiting or triggering cell apoptosis.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
基金Supported by the Science and Technology Foundation of Beijing Jiaotong University (Grant Nos. 2006RC035 and 2007XM047)
文摘DEK protein is an ubiquitous phosphorylated nuclear protein.Specific binding of DEK to DNA could change the topology of DNA and then affect the gene activity of the underlying DNA sequences.It is speculated that there might be some potential relationship between the stress reaction of cells and DEK proteins.The phosphorylation status of DEK protein is altered during death-receptor-mediated cell apoptosis.Both phosphorylation and poly(ADP-ribosyl)ation could promote the release of DEK from apoptotic nuclei to extracellular environment,and in this case DEK becomes a potential autoantigen of some autoimmune diseases.The available evidence powerfully suggests that DEK protein is closely relevant to apoptosis.The overexpression of DEK protein has dual function in cell apoptosis,in terms of inhibiting or triggering cell apoptosis.
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 partly supported by research grants No. 81072703 （to Dr. Yu） from the National Natural Science Foundation, Beijing, P.R. China, a research grant No. 10411951700 （to Dr. Zhang） from Science and Technology Commission of Shanghai Municipality, Shanghai, P.R. China.The authors confirm that there are no conflicts of interests.
