Fls2

Gómez-Gómez, Lourdes; Boller, Thomas

doi:10.1016/s1097-2765(00)80265-8

Cited by 1,921 publications

(496 citation statements)

References 50 publications

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“…One of the best-explored PTI-associated pattern recognition receptors (PRRs) in angiosperms is FLS2. FLS2 recognizes the microbe-associated molecular pattern (MAMP) flg22, a peptide component of the bacterial flagellin [56,67]. Orthologs of FLS2 were not found in the moss P. patens [68], although a homolog with appreciable sequence conservation was found [69].…”

Section: Pti and Eti In Non-flowering Land Plants And Maybe Streptophmentioning

confidence: 99%

On plant defense signaling networks and early land plant evolution

Vries

Dahlen

Gould

et al. 2018

Communicative & Integrative Biology

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All land plants must cope with phytopathogens. Algae face pathogens, too, and it is reasonable to assume that some of the strategies for dealing with pathogens evolved prior to the origin of embryophytes – plant terrestrialization simply changed the nature of the plant-pathogen interactions. Here we highlight that many potential components of the angiosperm defense toolkit are i) found in streptophyte algae and non-flowering embryophytes and ii) might be used in non-flowering plant defense as inferred from published experimental data. Nonetheless, the common signaling networks governing these defense responses appear to have become more intricate during embryophyte evolution. This includes the evolution of the antagonistic signaling pathways of jasmonic and salicylic acid, multiple independent expansions of resistance genes, and the evolution of resistance gene-regulating microRNAs. Future comparative studies will illuminate which modules of the streptophyte defense signaling network constitute the core and which constitute lineage- and/or environment-specific (peripheral) signaling circuits.

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Section: Pti and Eti In Non-flowering Land Plants And Maybe Streptophmentioning

confidence: 99%

On plant defense signaling networks and early land plant evolution

Vries

Dahlen

Gould

et al. 2018

Communicative & Integrative Biology

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“…Constructions of Chimeric Receptors between EFR and FLS2-FLS2, the receptor for bacterial flagellin FLS2 (13), is one of the closest relatives of EFR encoded in the A. thaliana genome. EFR and FLS2 both belong to the same subfamily XII of the LRRRLKs (26).…”

Section: N-and C-terminal Truncations Of Efr-as a First Step Inmentioning

confidence: 99%

“…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.…”

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...

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“…Bacterial flagellin triggers many defence responses via the perception of the immunogenic peptide of flagellin (flg22) by its cognate receptor FLS2 (Gómez‐Gómez & Boller, 2000). In Arabidopsis these responses include both the influx of Ca 2+ and plasmodesmal closure; Ca 2+ signalling is believed to be a critical component of a successful immune response (Lecourieux et al ., 2006; Seybold et al ., 2014).…”

Section: Introductionmentioning

confidence: 99%

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

et al. 2017

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Summary Plants sense microbial signatures via activation of pattern recognition receptors (PPRs), which trigger a range of cellular defences. One response is the closure of plasmodesmata, which reduces symplastic connectivity and the capacity for direct molecular exchange between host cells.Plasmodesmal flux is regulated by a variety of environmental cues but the downstream signalling pathways are poorly defined, especially the way in which calcium regulates plasmodesmal closure.Here, we identify that closure of plasmodesmata in response to bacterial flagellin, but not fungal chitin, is mediated by a plasmodesmal‐localized Ca2+‐binding protein Calmodulin‐like 41 (CML41). CML41 is transcriptionally upregulated by flg22 and facilitates rapid callose deposition at plasmodesmata following flg22 treatment. CML41 acts independently of other defence responses triggered by flg22 perception and reduces bacterial infection.We propose that CML41 enables Ca2+‐signalling specificity during bacterial pathogen attack and is required for a complete defence response against Pseudomonas syringae.

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Fls2

Cited by 1,921 publications

References 50 publications

On plant defense signaling networks and early land plant evolution

On plant defense signaling networks and early land plant evolution

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

A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses

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