Ubiquitin/Proteasome System in Plant Pathogen Responses

Sorel, Maud; Mooney, Brian; Marchi, Rémi de; Graciet, Emmanuelle

doi:10.1002/9781119312994.apr0665

Cited by 10 publications

(7 citation statements)

References 312 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, VAMPs, syntaxins, and ABC transporters have been found among the DEGs, but most of them have not been described as associated with plant immunity yet. In the same line, proteasome proteolytic pathway and ubiquitination play major roles in plant immunity (43,44). With the exception of RIN2 (RPM1 interacting protein 2) (45), 19 genes encoding ubiquitin-ligases or proteasome subunits have been identified in our study, most of them not previously described as involved in plant immunity.…”

Section: Discussionmentioning

confidence: 72%

Robustness of plant quantitative disease resistance is provided by a decentralized immune network

Delplace

Huard-Chauveau

Dubiella

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Quantitative disease resistance (QDR) represents the predominant form of resistance in natural populations and crops. Surprisingly, very limited information exists on the biomolecular network of the signaling machineries underlying this form of plant immunity. This lack of information may result from its complex and quantitative nature. Here, we used an integrative approach including genomics, network reconstruction, and mutational analysis to identify and validate molecular networks that control QDR in Arabidopsis thaliana in response to the bacterial pathogen Xanthomonas campestris. To tackle this challenge, we first performed a transcriptomic analysis focused on the early stages of infection and using transgenic lines deregulated for the expression of RKS1, a gene underlying a QTL conferring quantitative and broad-spectrum resistance to X. campestris. RKS1-dependent gene expression was shown to involve multiple cellular activities (signaling, transport, and metabolism processes), mainly distinct from effector-triggered immunity (ETI) and pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) responses already characterized in A. thaliana. Protein–protein interaction network reconstitution then revealed a highly interconnected and distributed RKS1-dependent network, organized in five gene modules. Finally, knockout mutants for 41 genes belonging to the different functional modules of the network revealed that 76% of the genes and all gene modules participate partially in RKS1-mediated resistance. However, these functional modules exhibit differential robustness to genetic mutations, indicating that, within the decentralized structure of the QDR network, some modules are more resilient than others. In conclusion, our work sheds light on the complexity of QDR and provides comprehensive understanding of a QDR immune network.

show abstract

Section: Discussionmentioning

confidence: 72%

Robustness of plant quantitative disease resistance is provided by a decentralized immune network

Delplace

Huard-Chauveau

Dubiella

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…The ubiquitin–proteasome system (UPS) in plants plays a critical role in mediating biotic stress responses not only through the removal of misfolded and defective proteins but also through the regulation of protein stability [ 157 , 158 ]. Proteins destined for degradation by the UPS are ubiquitinated by a cascade of three enzymatic reactions: (1) ubiquitin activation by the E1 enzyme; (2) transfer to the ubiquitin-conjugating enzyme, E2, and (3) attachment to the substrate by the E3 ligase [ 159 ].…”

Section: T3se Manipulation Of the Ubiquitin–proteasome Systemmentioning

confidence: 99%

What the Wild Things Do: Mechanisms of Plant Host Manipulation by Bacterial Type III-Secreted Effector Proteins

2021

View full text Add to dashboard Cite

Phytopathogenic bacteria possess an arsenal of effector proteins that enable them to subvert host recognition and manipulate the host to promote pathogen fitness. The type III secretion system (T3SS) delivers type III-secreted effector proteins (T3SEs) from bacterial pathogens such as Pseudomonas syringae, Ralstonia solanacearum, and various Xanthomonas species. These T3SEs interact with and modify a range of intracellular host targets to alter their activity and thereby attenuate host immune signaling. Pathogens have evolved T3SEs with diverse biochemical activities, which can be difficult to predict in the absence of structural data. Interestingly, several T3SEs are activated following injection into the host cell. Here, we review T3SEs with documented enzymatic activities, as well as T3SEs that facilitate virulence-promoting processes either indirectly or through non-enzymatic mechanisms. We discuss the mechanisms by which T3SEs are activated in the cell, as well as how T3SEs modify host targets to promote virulence or trigger immunity. These mechanisms may suggest common enzymatic activities and convergent targets that could be manipulated to protect crop plants from infection.

show abstract

“…The light was then revealed to induce degradation of phytochrome interacting factor PIF1 by the CUL4 COP1-SPA E3 ligase initiated photomorphogenesis [65]. Thereafter, the involvement of ubiquitylation in various plant signaling pathways has been broadly reported such as calcium signaling, 14-3-3 proteins and G-proteins mediated signaling [66,67].…”

Section: Ubiquitylation Coordinates Plant Signalingmentioning

confidence: 99%

Advances on Plant Ubiquitylome—From Mechanism to Application

Damaris

et al. 2020

IJMS

View full text Add to dashboard Cite

Post-translational modifications (PTMs) of proteins enable modulation of their structure, function, localization and turnover. To date, over 660 PTMs have been reported, among which, reversible PTMs are regarded as the key players in cellular signaling. Signaling mediated by PTMs is faster than re-initiation of gene expression, which may result in a faster response that is particularly crucial for plants due to their sessile nature. Ubiquitylation has been widely reported to be involved in many aspects of plant growth and development and it is largely determined by its target protein. It is therefore of high interest to explore new ubiquitylated proteins/sites to obtain new insights into its mechanism and functions. In the last decades, extensive protein profiling of ubiquitylation has been achieved in different plants due to the advancement in ubiquitylated proteins (or peptides) affinity and mass spectrometry techniques. This obtained information on a large number of ubiquitylated proteins/sites helps crack the mechanism of ubiquitylation in plants. In this review, we have summarized the latest advances in protein ubiquitylation to gain comprehensive and updated knowledge in this field. Besides, the current and future challenges and barriers are also reviewed and discussed.

show abstract

Ubiquitin/Proteasome System in Plant Pathogen Responses

Cited by 10 publications

References 312 publications

Robustness of plant quantitative disease resistance is provided by a decentralized immune network

Robustness of plant quantitative disease resistance is provided by a decentralized immune network

What the Wild Things Do: Mechanisms of Plant Host Manipulation by Bacterial Type III-Secreted Effector Proteins

Advances on Plant Ubiquitylome—From Mechanism to Application

Contact Info

Product

Resources

About