Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide

Morita, Junko; Kato, Kazuki; Nakane, Takanori; Kondo, Yuki; Fukuda, Hiroo; Nishimasu, Hiroshi; Ishitani, Ryuichiro; Nureki, Osamu

doi:10.1038/ncomms12383

Cited by 75 publications

(62 citation statements)

References 34 publications

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“…RPK2 contains two island domains that map to the N-terminal and central portions of its LRR domain, but their function is unknown (63,106,114). By contrast, most of the characterized peptide ligand LRR-RKs, such as HAESA, TDR/PXY, FLS2, and PEPR, do not contain island-domain structures (89,100,120,122,144). This suggests that plants may have evolved island-domain-containing LRR ectodomains to facilitate the specific binding of relatively small ligands.…”

Section: C)mentioning

confidence: 95%

“…The LRR-RKs CLAVATA 1 (CLV1), BARELY ANY MERISTEM 1-3 (BAM1-3), RECEPTOR-LIKE PROTEIN KINASE 2 (RPK2), and TRACHEARY ELEMENT DIFFERENTIATION FACTOR RECEPTOR/PHLOEM INTERCALATED WITH XYLEM (TDR/PXY) sense small, posttranslationally modified CLV3/EMBRYO SURROUNDING REGION (ESR)-RELATED (CLE) peptide hormones, including CLV3, to maintain plant stem cell populations in the shoot and in the root (24,30,32,33,45,88,89,106,114,145). A family of secreted peptide hormones with structural similarities to CLEs, the INFLORESCENCE DEFICIENT IN ABSCISSION-LIKE (IDL) peptides, trigger abscission and cell separation processes in plants by binding to the LRR-RKs HAESA and HAESA-LIKE 2 (HSL2) (15,67,100,126).…”

Section: Architecture Of Plant Receptor Kinases (Rks) Receptor-like mentioning

confidence: 99%

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The Structural Basis of Ligand Perception and Signal Activation by Receptor Kinases

Hohmann

Lau

Hothorn

2017

Annu. Rev. Plant Biol.

237

254

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Plants have evolved a family of unique membrane receptor kinases to orchestrate the growth and development of their cells, tissues, and organs. Receptor kinases also form the first line of defense of the plant immune system and allow plants to engage in symbiotic interactions. Here, we discuss recent advances in understanding, at the molecular level, how receptor kinases with lysin-motif or leucine-rich-repeat ectodomains have evolved to sense a broad spectrum of ligands. We summarize and compare the established receptor activation mechanisms for plant receptor kinases and dissect how ligand binding at the cell surface leads to activation of cytoplasmic signaling cascades. Our review highlights that one family of plant membrane receptors has diversified structurally to fulfill very different signaling tasks.

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Section: C)mentioning

confidence: 95%

Section: Architecture Of Plant Receptor Kinases (Rks) Receptor-like mentioning

confidence: 99%

The Structural Basis of Ligand Perception and Signal Activation by Receptor Kinases

Hohmann

Lau

Hothorn

2017

Annu. Rev. Plant Biol.

237

254

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“…The residues effected in these mutants are highly conserved among related LRR-RKs and structural and biochemical studies with PXY/TDIF receptor ligand pair have shown that these residues direct ligand binding [24–28]. In contrast, clv1 null mutants are significantly weaker [29].…”

Section: Introductionmentioning

confidence: 99%

CLAVATA1 controls distinct signaling outputs that buffer shoot stem cell proliferation through a two-step transcriptional compensation loop

Nimchuk

2017

PLoS Genet

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The regulation of stem cell proliferation in plants is controlled by intercellular signaling pathways driven by the diffusible CLAVATA3 (CLV3p) peptide. CLV3p perception is thought to be mediated by an overlapping array of receptors in the stem cell niche including the transmembrane receptor kinase CLV1, Receptor-Like Protein Kinase 2 (RPK2), and a dimer of the receptor-like protein CLV2 and the CORYNE (CRN) pseudokinase. Mutations in these receptors have qualitatively similar effects on stem cell function but it is unclear if this represents common or divergent signaling outputs. Previous work in heterologous systems has suggested that CLV1, RPK2 and CLV2/CRN could form higher order complexes but it is also unclear what relevance these putative complexes have to in vivo receptor functions. Here I use the in vivo regulation of a specific transcriptional target of CLV1 signaling in Arabidopsis to demonstrate that, despite the phenotypic similarities between the different receptor mutants, CLV1 controls distinct signaling outputs in living stem cell niches independent of other receptors. This regulation is separable from stem cell proliferation driven by WUSCHEL, a proposed common transcriptional target of CLV3p signaling. In addition, in the absence of CLV1, CLV1-related receptor kinases are ectopically expressed but also buffer stem cell proliferation through the auto-repression of their own expression. Collectively these data reveal a unique in vivo role for CLV1 separable from other stem cell receptors and provides a framework for dissecting the signaling outputs in stem cell regulation.

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“…Recently two papers have reported the structural studies of TDIF-TDR(PXY) interactions. In addition, structure-guided mutational studies in both reports have indicated a conserved binding mode between CLE peptides and their cognate LRR-RLK receptors centered on residue G6 of CLEs [27, 28]. However, further studies are entailed in order to understand the binding specificities of CLE ligands to different LRR-RLKs.…”

Section: Introductionmentioning

confidence: 99%

Differential CLE peptide perception by plant receptors implicated from structural and functional analyses of TDIF-TDR interactions

Chakraborty

2017

PLoS ONE

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Tracheary Element Differentiation Inhibitory Factor (TDIF) belongs to the family of post-translationally modified CLE (CLAVATA3/embryo surrounding region (ESR)-related) peptide hormones that control root growth and define the delicate balance between stem cell proliferation and differentiation in SAM (shoot apical meristem) or RAM (root apical meristem). In Arabidopsis, Tracheary Element Differentiation Inhibitory Factor Receptor (TDR) and its ligand TDIF signaling pathway is involved in the regulation of procambial cell proliferation and inhibiting its differentiation into xylem cells. Here we present the crystal structures of the extracellular domains (ECD) of TDR alone and in complex with its ligand TDIF resolved at 2.65 Ǻ and 2.75 Ǻ respectively. These structures provide insights about the ligand perception and specific interactions between the CLE peptides and their cognate receptors. Our in vitro biochemical studies indicate that the interactions between the ligands and the receptors at the C-terminal anchoring site provide conserved binding. While the binding interactions occurring at the N-terminal anchoring site dictate differential binding specificities between different ligands and receptors. Our studies will open different unknown avenues of TDR-TDIF signaling pathways that will enhance our knowledge in this field highlighting the receptor ligand interaction, receptor activation, signaling network, modes of action and will serve as a structure function relationship model between the ligand and the receptor for various similar leucine-rich repeat receptor-like kinases (LRR-RLKs).

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Crystal structure of the plant receptor-like kinase TDR in complex with the TDIF peptide

Cited by 75 publications

References 34 publications

The Structural Basis of Ligand Perception and Signal Activation by Receptor Kinases

The Structural Basis of Ligand Perception and Signal Activation by Receptor Kinases

CLAVATA1 controls distinct signaling outputs that buffer shoot stem cell proliferation through a two-step transcriptional compensation loop

Differential CLE peptide perception by plant receptors implicated from structural and functional analyses of TDIF-TDR interactions

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