NUcleoside Diphosphate-linked to moiety X(NUDIX)hydrolases are ubiquitous enzymes that maintain metabolic homeostasis by hydrolyzing potentially toxic nucleoside diphosphates.In plants and other eukaryotes,inositol py...NUcleoside Diphosphate-linked to moiety X(NUDIX)hydrolases are ubiquitous enzymes that maintain metabolic homeostasis by hydrolyzing potentially toxic nucleoside diphosphates.In plants and other eukaryotes,inositol pyrophosphates(PP-InsPs)act as central signaling molecules,linking cellular phosphate status to gene expression via SPX-domain receptors.A recent study(McCombe et al.,Science 387:955–962,2025)showed that several plant pathogenic fungi secrete NUDIX effector proteins that hydrolyze PP-InsPs and manipulate host phosphate signaling.In the blast fungus Magnaporthe oryzae,a cytoplasmic NUDIX effector(MoNUDIX)hydrolyzes PP-InsPs,triggers a phosphate starvation response and suppresses immunity in rice,thereby facilitating disease progression.In contrast,the lentil anthracnose pathogen Colletotrichum lentis secretes CtNUDIX into the apoplast,where it disrupts PP-InsP-dependent endocytic machinery and elicits a hypersensitive cell death response.Collectively,these findings demonstrate how NUDIX effectors exemplify mechanistic diversification within a single effector family:manipulating phosphate signaling promotes biotrophic colonization,whereas disrupting host membrane integrity induces a switch to necrotrophy.展开更多
基金supported by the National Natural Science Foundation of China(Grant No.32172363)the Chinese Universities Scientific Fund(Grant No.10092004).
文摘NUcleoside Diphosphate-linked to moiety X(NUDIX)hydrolases are ubiquitous enzymes that maintain metabolic homeostasis by hydrolyzing potentially toxic nucleoside diphosphates.In plants and other eukaryotes,inositol pyrophosphates(PP-InsPs)act as central signaling molecules,linking cellular phosphate status to gene expression via SPX-domain receptors.A recent study(McCombe et al.,Science 387:955–962,2025)showed that several plant pathogenic fungi secrete NUDIX effector proteins that hydrolyze PP-InsPs and manipulate host phosphate signaling.In the blast fungus Magnaporthe oryzae,a cytoplasmic NUDIX effector(MoNUDIX)hydrolyzes PP-InsPs,triggers a phosphate starvation response and suppresses immunity in rice,thereby facilitating disease progression.In contrast,the lentil anthracnose pathogen Colletotrichum lentis secretes CtNUDIX into the apoplast,where it disrupts PP-InsP-dependent endocytic machinery and elicits a hypersensitive cell death response.Collectively,these findings demonstrate how NUDIX effectors exemplify mechanistic diversification within a single effector family:manipulating phosphate signaling promotes biotrophic colonization,whereas disrupting host membrane integrity induces a switch to necrotrophy.
