The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity

Postel, Sandra; Küfner, Isabell; Beuter, Christine; Mazzotta, Sara; Schwedt, Anne; Borlotti, Andrea; Halter, Thierry; Kemmerling, Birgit; Nürnberger, Thorsten

doi:10.1016/j.ejcb.2009.11.001

Cited by 188 publications

(159 citation statements)

References 37 publications

Supporting

Mentioning

152

Contrasting

Unclassified

Order By: Relevance

“…While much less dense as compared to AtPep1-PEPR1LRR contacts mediated by the C-terminal portion of AtPep1, these non-conserved interactions are likely also important for AtPep1-induced signaling as AtPep1(14-23) is nearly inactive in inducing cell immune responses when tested at lower concentrations [15]. However, a higher concentration (25 nM) of the peptide, but not AtPep1 (15)(16)(17)(18)(19)(20)(21)(22)(23), displayed immunogenic activity, though lower than that of the wild-type peptide [15]. These results suggest that AtPep1 (14)(15) linking the conserved C-terminal and non-conserved N-terminal regions of AtPep1 may function as a hot spot for AtPep1-PEPR1LRR interaction.…”

Section: Recognition Of Atpep1 By Pepr1mentioning

confidence: 99%

“…Previous studies showed that AtPep1 binding induced PEPR1-BAK1 heteromerization [23,24]. However, in vitro reconstitution of an AtPep1-induced complex using purified proteins has not yet been reported.…”

Section: Reconstitution Of the Pepr1lrr-atpep1 And Pepr1l-rr-atpep1-bmentioning

confidence: 99%

“…Ca 2+ has been shown to be important for the AtPep/ PEPR signaling [21,22]. Similar to FLS2 and EFR, PEPR1 stably associates with BAK1 in response to treatment with AtPeps [23,24]. A number of studies suggest that PEPR-mediated immune responses serve to amplify PTI signaling [25][26][27][28] via the JA/ET (jasmonic acid-ethylene) and SA (salicylic acid) pathways [25,28].…”

Section: Introductionmentioning

confidence: 99%

“…A later study using alanine-scanning analysis showed that an AtPep1-derived peptide with the N-terminal deletion of eight amino acids, AtPep1 (9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23), is equally active as the wild-type peptide in inducing PTI-like responses [15]. AtPep1 and its homologs AtPep2-8 mature from the conserved C-terminal portion of their respective precursors PROPEP1-8, respectively [14,16].…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1

et al. 2014

View full text Add to dashboard Cite

The endogenous peptides AtPep1-8 in Arabidopsis mature from the conserved C-terminal portions of their precursor proteins PROPEP1-8, respectively. The two homologous leucine-rich repeat-receptor kinases (LRR-RKs) PEPR1 and PEPR2 act as receptors of AtPeps. AtPep binding leads to stable association of PEPR1,2 with the shared receptor LRR-RK BAK1, eliciting immune responses similar to those induced by pathogens. Here we report a crystal structure of the extracellular LRR domain of PEPR1 (PEPR1LRR) in complex with AtPep1. The structure reveals that AtPep1 adopts a fully extended conformation and binds to the inner surface of the superhelical PEPR1LRR. Biochemical assays showed that AtPep1 is capable of inducing PEPR1LRR-BAK1LRR heterodimerization. The conserved C-terminal portion of AtPep1 dominates AtPep1 binding to PEPR1LRR, with the last amino acid of AtPep1 Asn23 forming extensive interactions with PEPR1LRR. Deletion of the last residue of AtPep1 significantly compromised AtPep1 interaction with PEPR1LRR. Together, our data reveal a conserved structural mechanism of AtPep1 recognition by PEPR1, providing significant insight into prediction of recognition of other peptides by their cognate LRR-RKs.

show abstract

Section: Recognition Of Atpep1 By Pepr1mentioning

confidence: 99%

Section: Reconstitution Of the Pepr1lrr-atpep1 And Pepr1l-rr-atpep1-bmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1

et al. 2014

View full text Add to dashboard Cite

show abstract

“…29,30 In its role as coreceptor, BAK1 is thought to bind to the receptor kinase in a ligand-dependent manner, and to then autophosphorylate and also transphosphorylate sites on the receptor kinase. 2 How the various functions and interactions of BAK1 are regulated is not known but conceivably site-specific (auto) phosphorylation could play a role.…”

Section: Phosphorylation Of Bak1 At the Tyr-610 Site Is Essential Formentioning

confidence: 99%

Functional importance of BAK1 tyrosine phosphorylation in vivo

Clouse

2011

Plant Signaling & Behavior

View full text Add to dashboard Cite

Glucose and Brassinosteroid Signaling Network in Controlling Plant Growth and Development Under Different Environmental Conditions

Singh

Gupta

Laxmi

2017

Mechanism of Plant Hormone Signaling Under Stress

View full text Add to dashboard Cite

The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity

Cited by 188 publications

References 37 publications

Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1

Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1

Functional importance of BAK1 tyrosine phosphorylation in vivo

Glucose and Brassinosteroid Signaling Network in Controlling Plant Growth and Development Under Different Environmental Conditions

Contact Info

Product

Resources

About