E3 ubiquitin-ligases and their target proteins during the regulation of plant innate immunity

被引:157
作者
Duplan, Vincent [1 ,2 ]
Rivas, Susana [1 ,2 ]
机构
[1] INRA, LIPM, UMR441, F-31326 Castanet Tolosan, France
[2] CNRS, LIPM, UMR2594, F-31326 Castanet Tolosan, France
来源
FRONTIERS IN PLANT SCIENCE | 2014年 / 5卷
关键词
E3; ubiquitin-ligase; microbial effector; plant immunity; 26S proteasome; ubiquitination; RECOGNITION RECEPTOR FLS2; PROGRAMMED CELL-DEATH; DISEASE RESISTANCE; TRIGGERED IMMUNITY; STRESS RESPONSES; EFFECTOR AVR3A; ARABIDOPSIS; ACTIVATION; DEGRADATION; PATHOGEN;
D O I
10.3389/fpls.2014.00042
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Reversible protein ubiquitination plays a crucial role during the regulation of plant immune signaling. E3 ubiquitin (Ub)-ligase enzymes, which are classified into different families depending on their structural and functional features, confer the specificity of substrate and are the best characterized components of the ubiquitination cascade. E3 Ub-ligases of different families have been shown to be involved in all steps of plant immune responses. Indeed, they have been involved in the first steps of pathogen perception, as they appear to modulate perception of pathogen-associated molecular patterns by pattern-recognition receptors at the plasma membrane and to regulate the accumulation of nucleotide-binding leucine-rich repeat-type intracellular immune receptors. In addition, E3 Ub-ligase proteins are also involved in the regulation of the signaling responses downstream of pathogen perception through targeting vesicle trafficking components or nuclear transcription factors, for instance. Finally, we also discuss the case of microbial effector proteins that are able to target host E3 Ub-ligases, or to act themselves as E3 Ub-ligases, in their attempt to subvert the host proteasome to promote disease.
引用
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页数:6
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