Comparative Analysis of the Receptor-Like Kinase Family in Arabidopsis and Rice[W]

Shiu, Shin-Han; Karłowski, Wojciech M.; Pan, Runsun; Tzeng, Yun-Huei; Mayer, Klaus; Li, Wen-Hsiung

doi:10.1105/tpc.020834

Cited by 1,015 publications

(1,082 citation statements)

References 88 publications

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“…BRI1 and BAK1 belong to a large family of plant-specific LRR-RLKs, consisting of more than 200 members in Arabidopsis and over 300 in rice [31]. Three close homologs of BRI1 have been characterized [19,20,32].…”

Section: Tissue Specific Functions Of the Homologs Of Bri1 And Bak1mentioning

confidence: 99%

The brassinosteroid signal transduction pathway

Wang

Chong

et al. 2006

Cell Res

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Steroids function as signaling molecules in both animals and plants. While animal steroid hormones are perceived by nuclear receptor family of transcription factors, brassinosteroids (BR) in plants are perceived by a cell surface receptor kinase, BRI1. Recent studies have demonstrated that BR binding to the extracellular domain of BRI1 induces kinase activation and dimerization with another receptor kinase, BAK1. Activated BRI1 or BAK1 then regulate, possibly indirectly, the activities of BIN2 kinase and/or BSU1 phosphatase, which directly regulate the phosphorylation status and nuclear accumulation of two homologous transcription factors, BZR1 and BES1. BZR1 and BES1 directly bind to promoters of BR responsive genes to regulate their expression. The BR signaling pathway has become a paradigm for both receptor kinase signaling in plants and steroid signaling by cell surface receptors in general.

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Section: Tissue Specific Functions Of the Homologs Of Bri1 And Bak1mentioning

confidence: 99%

The brassinosteroid signal transduction pathway

Wang

Chong

et al. 2006

Cell Res

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“…3B) there is little sequence homology outside these regions. This is surprising because it is the relatedness of the kinase sequences that was used to place EFR and FLS2 into the same subfamily XII of the LRR receptor like kinases (family 1.12.4 in PlantsP Kinase classification) (2). EFR and FLS2 trigger the same signal outputs leading to a congruent set of responses (14).…”

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

confidence: 99%

“…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.…”

mentioning

confidence: 99%

“…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).…”

mentioning

confidence: 99%

“…E-mail: georg.felix@ uni-tuebingen.de. 2 The abbreviations used are: RLK, receptor-like kinase; FLS2, flagellin-sensing 2; MAMP, microbe-associated molecular pattern; EF-Tu, elongation factor Tu; LRR, leucine-rich repeat; GFP, green fluorescent protein; MES, 4-morpholineethanesulfonic acid. …”

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confidence: 99%

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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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Alternative splicing of the receptor‐like kinase Nt‐Sd‐RLK in tobacco cells responding to lipopolysaccharides: suggestive of a role in pathogen surveillance and perception?

Sanabria

Dubery

2016

FEBS Letters

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Nt-Sd-RLK encodes an S-domain lectin receptor-like kinase that is induced in response to microbe-associated molecular pattern molecules (MAMPs) such as lipopolysaccharide (LPS). In this study, we investigated the alternative splicing of Nt-Sd-RLK in response to LPS stimulation. Our data indicate that in nonstimulated cells, a shorter transcript of Nt-Sd-RLK is generated and that in response to LPS, alternative splicing produces the full-length transcript. We propose that the extracellular domain of Nt-Sd-RLK encoded by the shorter transcript functions in pathogen surveillance. Once this domain binds LPS, alternative splicing generates the kinase domain-containing Nt-Sd-RLK that activates downstream signalling leading to a defence response. Thus, our findings suggest that plant defence signalling may be regulated through the alternative splicing of receptor-like kinases involved in pathogen recognition.

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Comparative Analysis of the Receptor-Like Kinase Family in Arabidopsis and Rice[W]

Cited by 1,015 publications

References 88 publications

The brassinosteroid signal transduction pathway

The brassinosteroid signal transduction pathway

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

Alternative splicing of the receptor‐like kinase Nt‐Sd‐RLK in tobacco cells responding to lipopolysaccharides: suggestive of a role in pathogen surveillance and perception?

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