Plant Receptor-like proteins (RLPs): Structural features enabling versatile immune recognition

Snoeck, Simon; Garcia, Anthony G. K.; Steinbrenner, Adam D.

doi:10.1016/j.pmpp.2023.102004

Cited by 15 publications

(10 citation statements)

References 99 publications

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“…Furthermore, our data suggest that MtSOBIR1 can contribute to an immuneassociated response to plant pathogens in roots. The question then is whether MtSOBIR1 and MtNFP intervene together for their roles in immunity against root pathogens like A. euteiches, especially given that SOBIR1 has only ever been reported to interact with RLKs/RLPs with LRR domains (Snoeck et al 2023). Firstly, we confirmed that MtSOBIR1 is well expressed in roots and root hairs, like MtNFP, which is compatible with a role of MtSOBIR1 together with MtNFP in early root-pathogen interactions.…”

Section: Do Mtnfp and Mtsobir1 Intervene Together In The Control Of P...supporting

confidence: 78%

“…SOBIR1 proteins are well known co-receptors, and their roles generally involve complex formation with other receptors, notably RLPs (Gust and Felix 2014) (Snoeck et al 2023), although some SOBIR1-RLCK interactions have also been reported (Pruitt et al 2021). SOBIR1 interactors are generally involved in immunity, but SOBIR1 can also interact with development-related RLPs such as CLV2 and TMM (Liebrand et al 2014), and, although the mechanism is not clear, SOBIR1 is a negative regulator of the HAES/HAESA-like2 pathway for organ abscission (Gubert and Liljegren 2014).…”

Section: Discussionmentioning

confidence: 99%

“…SOBIR1 interactors are generally involved in immunity, but SOBIR1 can also interact with development-related RLPs such as CLV2 and TMM (Liebrand et al 2014), and, although the mechanism is not clear, SOBIR1 is a negative regulator of the HAES/HAESA-like2 pathway for organ abscission (Gubert and Liljegren 2014). Gx 3 G motifs in the TM of SOBIR1 proteins, and in interacting RLPs, are important for the interactions of these proteins (Bi et al 2016); (Snoeck et al 2023). This region of MtSOBIR1 is highly conserved with that of AtSOBIR1 (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Some of the other phospho-sites on LjNFR5-KD identified with LjSYMRK-KD, as well as 9 predicted phospho sites on MtNFP, have all been shown to be nonessential when tested in complementation tests (Madsen et al 2011) (Lefebvre et al 2012), underlining the difficulty of finding biologically relevant phospho sites in these proteins using these techniques. SOBIR1 proteins are well known co-receptors, and their roles generally involve complex formation with other receptors, notably RLPs (Gust and Felix 2014) (Snoeck et al 2023), although some SOBIR1-RLCK interactions have also been reported (Pruitt et al 2021). SOBIR1 interactors are generally involved in immunity, but SOBIR1 can also interact with development-related RLPs such as CLV2 and TMM (Liebrand et al 2014), and, although the mechanism is not clear, SOBIR1 is a negative regulator of the HAES/HAESA-like2 pathway for organ abscission (Gubert and Liljegren 2014).…”

Section: The Mtsobir1-mtnfp Interactionmentioning

confidence: 99%

“…SOBIR1/EVR has an active kinase domain that can auto-phosphorylate on Serine/Threonine and Tyrosine residues in vitro (Leslie et al ., 2010) (Mitra et al 2015) (Wei et al 2022). Further studies on SOBIR1, including in other plants, have shown that it is a common coreceptor for many different LRR - receptor-like proteins (RLPs) which lack an intracellular signalling domain (Liebrand et al ., 2014; (Snoeck, Garcia, and Steinbrenner 2023). SOBIR1 can also interact in tripartite complexes that include the BRASSINOSTEROID INSENSITIVE1-ASSOCIATED RECEPTOR KINASE1 (BAK1) (Albert et al 2015)((van der Burgh et al 2019).…”

Section: Introductionmentioning

confidence: 99%

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Medicago truncatulaSOBIR1 controls specificity in the Rhizobium-legume symbiosis

Sarrette,

Luu,

Johansson

et al. 2023

Preprint

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Medicago truncatula Nod Factor Perception (MtNFP) is a lysin-domain Receptor-Like Kinase (LysM-RLK) that plays a key role in the Rhizobium-legume symbiosis, and is involved in plant immunity. MtNFP also has an inactive kinase domain, suggesting that the protein is involved in different receptor complexes. Using the MtNFP pseudo-kinase domain as a bait in a Yeast two Hybrid screen, we identified M. truncatula SUPPRESSOR OF BIR1 (MtSOBIR1) as a new interactor of MtNFP. We showed that an interaction between the two RLKs can occur in planta and that the kinase domain of MtSOBIR1 is active and can transphosphorylate the pseudo-kinase domain of MtNFP. Like in other plants, our data suggest a positive role of MtSOBIR1 in immunity; MtSOBIR1 could functionally complement an Atsobir1 mutant for defence activation, and a Mtsobir1 mutant was defective in pathogen-induced defence gene expression. We also showed that MtSOBIR1 has a symbiotic role with Mtsobir1 mutants showing a strong symbiotic phenotype in a plant genotype- and rhizobial strain-specific manner. The symbiotic role was apparent both at an early stage of rhizobial infection and in nodules. Together, these data suggest that, like MtNFP, MtSOBIR1 has a dual role, and can control immunity in both pathogenic and beneficial situations, with positive or negative roles, respectively.

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Section: Do Mtnfp and Mtsobir1 Intervene Together In The Control Of P...supporting

confidence: 78%