Phosphorylation-Regulated Activation of the Arabidopsis RRS1-R/RPS4 Immune Receptor Complex Reveals Two Distinct Effector Recognition Mechanisms

Guo, Hailong; Ahn, Hee-Kyung; Sklenář, Jan; Huang, Jianhua; Ma, Yan; Ding, Pingtao; Menke, Frank L. H.; Jones, Jonathan D. G.

doi:10.1016/j.chom.2020.03.008

Cited by 50 publications

(35 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, pentameric oligomerization of the CNL Hrp-dependent outer protein (Hop) Z-Activated Resistance 1, termed the “HopZ-Activated Resistance 1 resistosome”, is important for the formation of putative membrane pores and the immune response [ 67 ]. Similarly, several well-studied plant NLRs containing TIR domains, such as RECOGNITION OF PERONOSPORA PARASITICA 1 (RPP1), the flax resistance protein L6, RRS1, and RPS4, were found to require oligomerization by two distinct interfaces, for both self-association and defense signaling [ 68 , 69 , 70 , 71 , 72 ]. Similar to the case of MLA10, disrupting the homo-dimerization of L6 TIRs interferes with downstream signaling ( Figure 2 B).…”

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

“…On the other hand, a post-translational modification of one effector target can antagonize another. The newest report of RRS1/RPS4-mediated immunity revealed that phosphorylation regulates the activation of paired RRS1/RPS4 [ 71 ]. In the absence of effector AvrRps4 or PopP2, phosphorylation at threonine 1214 in the integrated decoy WRKY domain keeps RRS1 from the resistant ecotype Wassilewskija, in a resting state.…”

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

“…Dephosphorylation at that residue leads to the autoactivation of RRS1. Interestingly, PopP2 induces O-acetylation in the WRKY domain of RRS1, which competes with its phosphorylation and results in the dephosphorylated activated RRS1-mediated resistance to Ralstonia Solanacearum [ 71 ]. Other phosphorylation sites at the C terminus of RRS1 are required for PopP2 recognition, which enhances the interaction of the TIR domain with the WRKY domain.…”

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

“…However, RRS1-mediated resistance to the Pseudomonas syringae effector AvrRps4 is determined by the association of the RRS1 C-terminus with its TIR, not by its phosphorylation status [ 71 ]. The C terminus and TIR of RRS1 interact with each other only in the presence of AvrRps4 [ 71 ]. During recognition of AvrRps4 or PopP2, the interaction of the RRS1 TIR domain with its C terminus is enhanced.…”

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

“…The regulation of guardee/decoy monitoring is likely much more complex than is presently known. An additional 83 amino acids at the C-terminus of RRS1 from resistant ecotypes can function as a kinase docking site [ 71 ], suggesting that recruiting kinase protein activity or other post-translational modification could be involved in the RRS1/RPS4 activation.…”

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

See 4 more Smart Citations

Recent Advances in Effector-Triggered Immunity in Plants: New Pieces in the Puzzle Create a Different Paradigm

Nguyen

Iswanto

Son

et al. 2021

IJMS

View full text Add to dashboard Cite

Plants rely on multiple immune systems to protect themselves from pathogens. When pattern-triggered immunity (PTI)—the first layer of the immune response—is no longer effective as a result of pathogenic effectors, effector-triggered immunity (ETI) often provides resistance. In ETI, host plants directly or indirectly perceive pathogen effectors via resistance proteins and launch a more robust and rapid defense response. Resistance proteins are typically found in the form of nucleotide-binding and leucine-rich-repeat-containing receptors (NLRs). Upon effector recognition, an NLR undergoes structural change and associates with other NLRs. The dimerization or oligomerization of NLRs signals to downstream components, activates “helper” NLRs, and culminates in the ETI response. Originally, PTI was thought to contribute little to ETI. However, most recent studies revealed crosstalk and cooperation between ETI and PTI. Here, we summarize recent advancements in our understanding of the ETI response and its components, as well as how these components cooperate in the innate immune signaling pathways. Based on up-to-date accumulated knowledge, this review provides our current perspective of potential engineering strategies for crop protection.

show abstract

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

Section: Nlr Activation and Signaling Events Following Pathogen Recognitionmentioning

confidence: 99%

See 3 more Smart Citations

Recent Advances in Effector-Triggered Immunity in Plants: New Pieces in the Puzzle Create a Different Paradigm

Nguyen

Iswanto

Son

et al. 2021

IJMS

View full text Add to dashboard Cite

show abstract

PhosBoost: Improved phosphorylation prediction recall using gradient boosting and protein language models

Poretsky,

Andorf,

Sen

2023

Plant Direct

View full text Add to dashboard Cite

Protein phosphorylation is a dynamic and reversible post‐translational modification that regulates a variety of essential biological processes. The regulatory role of phosphorylation in cellular signaling pathways, protein–protein interactions, and enzymatic activities has motivated extensive research efforts to understand its functional implications. Experimental protein phosphorylation data in plants remains limited to a few species, necessitating a scalable and accurate prediction method. Here, we present PhosBoost, a machine‐learning approach that leverages protein language models and gradient‐boosting trees to predict protein phosphorylation from experimentally derived data. Trained on data obtained from a comprehensive plant phosphorylation database, qPTMplants, we compared the performance of PhosBoost to existing protein phosphorylation prediction methods, PhosphoLingo and DeepPhos. For serine and threonine prediction, PhosBoost achieved higher recall than PhosphoLingo and DeepPhos (.78, .56, and .14, respectively) while maintaining a competitive area under the precision‐recall curve (.54, .56, and .42, respectively). PhosphoLingo and DeepPhos failed to predict any tyrosine phosphorylation sites, while PhosBoost achieved a recall score of .6. Despite the precision‐recall tradeoff, PhosBoost offers improved performance when recall is prioritized while consistently providing more confident probability scores. A sequence‐based pairwise alignment step improved prediction results for all classifiers by effectively increasing the number of inferred positive phosphosites. We provide evidence to show that PhosBoost models are transferable across species and scalable for genome‐wide protein phosphorylation predictions. PhosBoost is freely and publicly available on GitHub.

show abstract

Structural basis of NLR activation and innate immune signalling in plants

et al. 2022

View full text Add to dashboard Cite

Animals and plants have NLRs (nucleotide-binding leucine-rich repeat receptors) that recognize the presence of pathogens and initiate innate immune responses. In plants, there are three types of NLRs distinguished by their N-terminal domain: the CC (coiled-coil) domain NLRs, the TIR (Toll/interleukin-1 receptor) domain NLRs and the RPW8 (resistance to powdery mildew 8)-like coiled-coil domain NLRs. CC-NLRs (CNLs) and TIR-NLRs (TNLs) generally act as sensors of effectors secreted by pathogens, while RPW8-NLRs (RNLs) signal downstream of many sensor NLRs and are called helper NLRs. Recent studies have revealed three dimensional structures of a CNL (ZAR1) including its inactive, intermediate and active oligomeric state, as well as TNLs (RPP1 and ROQ1) in their active oligomeric states. Furthermore, accumulating evidence suggests that members of the family of lipase-like EDS1 (enhanced disease susceptibility 1) proteins, which are uniquely found in seed plants, play a key role in providing a link between sensor NLRs and helper NLRs during innate immune responses. Here, we summarize the implications of the plant NLR structures that provide insights into distinct mechanisms of action by the different sensor NLRs and discuss plant NLR-mediated innate immune signalling pathways involving the EDS1 family proteins and RNLs.

show abstract

Phosphorylation-Regulated Activation of the Arabidopsis RRS1-R/RPS4 Immune Receptor Complex Reveals Two Distinct Effector Recognition Mechanisms

Cited by 50 publications

References 55 publications

Recent Advances in Effector-Triggered Immunity in Plants: New Pieces in the Puzzle Create a Different Paradigm

Recent Advances in Effector-Triggered Immunity in Plants: New Pieces in the Puzzle Create a Different Paradigm

PhosBoost: Improved phosphorylation prediction recall using gradient boosting and protein language models

Structural basis of NLR activation and innate immune signalling in plants

Contact Info

Product

Resources

About