The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants

Heese, Antje; Hann, Dagmar R.; Giménez-Ibáñez, Selena; Jones, Alexandra M. E.; He, Kongwang; Li, Jia; Schroeder, Julian I.; Peck, Scott C.; Rathjen, John P.

doi:10.1073/pnas.0705306104

Cited by 971 publications

(1,042 citation statements)

References 47 publications

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“…Recognition of different pathogen-derived MAMPs has been shown to elicit similar cellular responses, suggesting an early point of convergence in the corresponding signaling pathways. Recently, the receptor-like kinase BAK1 (brassinosteroid-associated kinase 1) was identified as a potentially important regulator in this signaling convergence [56 ].…”

Section: Resultsmentioning

confidence: 99%

Plant immune responses triggered by beneficial microbes

Wees

Ent

Pieterse

2008

Current Opinion in Plant Biology

732

494

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This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues.Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. In most cases authors

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Section: Resultsmentioning

confidence: 99%

Plant immune responses triggered by beneficial microbes

Wees

Ent

Pieterse

2008

Current Opinion in Plant Biology

732

494

View full text Add to dashboard Cite

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“…Moreover, both the FLS2 kinase domain and Pto bind AvrPto in a competitive manner, supporting structural similarity between FLS2-AvrPto and Pto-AvrPto interaction (Xiang et al, 2008). Interestingly, AvrPto also appears to bind BAK1 (Shan et al, 2008), a protein required for FLS2 and EFR1 function (Chinchilla et al, 2007;Heese et al, 2007).…”

Section: Introductionmentioning

confidence: 83%

Crystal Structure of the Complex between Pseudomonas Effector AvrPtoB and the Tomato Pto Kinase Reveals Both a Shared and a Unique Interface Compared with AvrPto-Pto

et al. 2009

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Resistance to bacterial speck disease in tomato (Solanum lycopersicum) is activated upon recognition by the host Pto kinase of either one of two sequence-unrelated effector proteins, AvrPto or AvrPtoB, from Pseudomonas syringae pv tomato (Pst). Pto induces Pst immunity by acting in concert with the Prf protein. The recently reported structure of the AvrPto-Pto complex revealed that interaction of AvrPto with Pto appears to relieve an inhibitory effect of Pto, allowing Pto to activate Prf. Here, we present the crystal structure of the Pto binding domain of AvrPtoB (residues 121 to 205) at a resolution of 1.9Å and of the AvrPtoB121-205–Pto complex at a resolution of 3.3 Å. AvrPtoB121-205 exhibits a tertiary fold that is completely different from that of AvrPto, and its conformation remains largely unchanged upon binding to Pto. In common with AvrPto-Pto, the AvrPtoB-Pto complex relies on two interfaces. One of these interfaces is similar in both complexes, although the primary amino acid sequences from the two effector proteins are very different. Amino acid substitutions in Pto at the other interface disrupt the interaction of AvrPtoB-Pto but not that of AvrPto-Pto. Interestingly, substitutions in Pto affecting this unique interface also cause Pto to induce Prf-dependent host cell death independently of either effector protein.

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Section: Transient Expression Of Tagged Versions Of Efr and Efr Lackimentioning

confidence: 99%

“…Upon activation with their respective ligands, FLS2, EFR, and AtPEPR1 seem to form heteromeric complexes with the co-receptor BAK1. Thus, intriguingly, BAK1 appears to function in the transmembrane signaling of plant RLKs with very different signal output programs (17)(18)(19)(20).The receptor kinase EFR from A. thaliana responds to bacterial elongation factor Tu (EF-Tu) with the induction of defense and increased resistance (14, 21). Mutant plants lacking this perception system show increased susceptibility to infection by Agrobacterium tumefaciens.…”

mentioning

confidence: 99%

Arabidopsis thaliana Pattern Recognition Receptors for Bacterial Elongation Factor Tu and Flagellin Can Be Combined to Form Functional Chimeric Receptors

Albert

Jehle

Mueller

et al. 2010

Journal of Biological Chemistry

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The receptor kinase EFR of Arabidopsis thaliana detects the microbe-associated molecular pattern elf18, a peptide that represents the N terminus of bacterial elongation factor Tu. Here, we tested subdomains of EFR for their importance in receptor function. Receptor-like kinases (RLKs) 2 form the biggest family of surface receptors in higher plants. Based on genomic sequence information, more than 600 genes in Arabidopsis thaliana and more than 1,000 genes in rice are predicted to encode RLKs (1, 2). RLKs have a common molecular structure consisting of a C-terminal cytoplasmic Ser/Thr protein kinase domain connected by a single-pass transmembrane motif to different types of N-terminal ectodomains facing extracytoplasmic compartments. Members of the RLK family play fundamental roles for cellular response programs regulating cell growth, morphogenesis, fertilization, abscission, plant defense, and interaction with symbionts (3-7). Nevertheless, the attribute "receptor-like" holds for most of the RLKs that still remain orphan with respect to their biological functions and their potential regulatory ligands. Concerning functional aspects of ligand interaction and transmembrane activation, the receptor kinase BRI1, functioning as the receptor for the growth hormone brassinolide, has been most thoroughly studied (8 -10). Thereby, the ligand interaction site could be localized to a small subdomain within the ectodomain of BRI1 (11), and activation was found to involve a ligand-dependent complex formation with a second receptor kinase termed BAK1 for BRI1-associated receptor kinase 1 (9, 10). Transient expression of tagged versions of EFR and EFR lacking its cytoplasmic domain in leaves ofSeveral RLKs have been assigned roles in recognition of pathogen attack. Examples for RLKs that function as pattern recognition receptors for identified ligands include XA21 from rice (12), FLS2 (13), EFR (14), and CERK1 (15) detecting microbe-associated molecular patterns (MAMPs), and AtPEPR1 (16) detecting wound-related, endogenous danger signals. Upon activation with their respective ligands, FLS2, EFR, and AtPEPR1 seem to form heteromeric complexes with the co-receptor BAK1. Thus, intriguingly, BAK1 appears to function in the transmembrane signaling of plant RLKs with very different signal output programs (17)(18)(19)(20).The receptor kinase EFR from A. thaliana responds to bacterial elongation factor Tu (EF-Tu) with the induction of defense and increased resistance (14, 21). Mutant plants lacking this perception system show increased susceptibility to infection by Agrobacterium tumefaciens. The epitope that acts as MAMP was identified as the acetylated N terminus of EF-Tu. Synthetic peptides like elf18 and elf26 which represent the N terminus of EF-Tu with at least 18 amino acids are fully active as MAMPs and stimulate responses at subnanomolar concentrations. A radiolabeled derivative of elf26 was used to demonstrate specific, high affinity binding sites in tissues expressing EFR. In affinity cross-linking experiments this radioli...

show abstract

The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants

Cited by 971 publications

References 47 publications

Plant immune responses triggered by beneficial microbes

Plant immune responses triggered by beneficial microbes

Crystal Structure of the Complex between Pseudomonas Effector AvrPtoB and the Tomato Pto Kinase Reveals Both a Shared and a Unique Interface Compared with AvrPto-Pto

Arabidopsis thaliana Pattern Recognition Receptors for Bacterial Elongation Factor Tu and Flagellin Can Be Combined to Form Functional Chimeric Receptors

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