A group of receptor kinases are essential for CLAVATA signalling to maintain stem cell homeostasis

Hu, Chong; Zhu, Yafen; Cui, Yanwei; Cheng, Kaili; Liang, Wei; Wei, Zhuoyun; Zhu, Mingsong; Yin, Hengfu; Zeng, Li; Xiao, Ye; Lv, Mei; Yi, Jing; Hou, Suiwen; He, Kongwang; Li, Jia; Gou, Xiaoping

doi:10.1038/s41477-018-0123-z

Cited by 156 publications

(156 citation statements)

References 31 publications

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“…Peptide hormones in plants are almost exclusively perceived by LRR family receptor kinases and receptor‐like proteins through the formation of homomers or heteromers (Hirakawa et al 2017). Genetic and biochemical assays showed that CLERK functions redundantly with three closely related LRR receptor kinases, CIK1, CIK3 and CIK4, to maintain stem cell homeostasis in the SAM (Hu et al 2018). CLV2 that interacts with CRN regulates stem cell homeostasis in the SAM through sensing the CLV3 peptide (Bleckmann et al 2010; Zhu et al 2010).…”

Section: Discussionmentioning

confidence: 99%

CLE25 peptide regulates phloem initiation in Arabidopsis through a CLERK‐CLV2 receptor complex

Ren

Song

Chen

et al. 2019

JIPB

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The phloem, located within the vascular system, is critical for delivery of nutrients and signaling molecules throughout the plant body. Although the morphological process and several factors regulating phloem differentiation have been reported, the molecular mechanism underlying its initiation remains largely unknown. Here, we report that the small peptide‐coding gene, CLAVATA 3 (CLV3)/EMBEYO SURROUNDING REGION 25 (CLE25), the expression of which begins in provascular initial cells of 64‐cell‐staged embryos, and continues in sieve element‐procambium stem cells and phloem lineage cells, during post‐embryonic root development, facilitates phloem initiation in Arabidopsis. Knockout of CLE25 led to delayed protophloem formation, and in situ expression of an antagonistic CLE25G6T peptide compromised the fate‐determining periclinal division of the sieve element precursor cell and the continuity of the phloem in roots. In stems of CLE25G6T plants the phloem formation was also compromised, and procambial cells were over‐accumulated. Genetic and biochemical analyses indicated that a complex, consisting of the CLE‐RESISTANT RECEPTOR KINASE (CLERK) leucine‐rich repeat (LRR) receptor kinase and the CLV2 LRR receptor‐like protein, is involved in perceiving the CLE25 peptide. Similar to CLE25, CLERK was also expressed during early embryogenesis. Taken together, our findings suggest that CLE25 regulates phloem initiation in Arabidopsis through a CLERK‐CLV2 receptor complex.

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Section: Discussionmentioning

confidence: 99%

CLE25 peptide regulates phloem initiation in Arabidopsis through a CLERK‐CLV2 receptor complex

Ren

Song

Chen

et al. 2019

JIPB

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“…SERKs as essential co-receptor kinases (Hu et al, 2018;Cui et al, 2018;Anne et al, 2018;Smakowska-Luzan et al, 2018;Zhang et al, 2017).…”

Section: Recent Genetic Biochemical and Structural Evidence Suggest mentioning

confidence: 99%

Constitutive activation of leucine-rich repeat receptor kinase signaling pathways by BAK1-interacting receptor-like kinase 3 chimera

Hohmann

Ramakrishna

Wang

et al. 2020

Preprint

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194 words) Receptor kinases with extracellular leucine-rich repeat domains (LRR-RKs) form the largest group of membrane signaling proteins in plants. LRR-RKs can sense small molecule, peptide or protein ligands, and may be activated by ligand-induced interaction with a shape complementary SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) coreceptor kinase. We have previously shown that SERKs can also form constitutive, ligandindependent complexes with the LRR ectodomains of BAK1-interacting receptor-like kinase 3 (BIR3) receptor pseudokinases, negative regulators of LRR-RK signaling. Here we report that receptor chimaera in which the extracellular LRR domain of BIR3 is fused to the cytoplasmic kinase domains of the SERK-dependent LRR-RKs BRASSINOSTEROID INSENSITIVE1, HAESA and ERECTA form tight complexes with endogenous SERK co-receptors in the absence of ligand stimulus. Expression of these chimaera under the control of the endogenous promoter of the respective LRR-RK leads to strong gain-of-function brassinosteroid, floral abscission and stomatal patterning phenotypes, respectively. Importantly, a BIR3-GSO1/SGN3 chimera can partially complement sgn3 Casparian strip formation phenotypes, suggesting that GSO1/SGN3 receptor activation is also mediated by SERK proteins. Collectively, our protein engineering approach may be used to elucidate the physiological functions of orphan LRR-RKs and to identify their receptor activation mechanism in single transgenic lines. 2 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 MAP kinase signaling pathway (Meng et al., 2015) with diverse roles in plant development involvesthe LRR-RK ERECTA (ER) and its paralogs ERECTA-LIKE1 (ERL1) and ERL2 (Torii et al., 1996;Shpak, 2013). ER, ERL1 and ERL2 together control stomata development and their correct spacing on the leaf surface (Shpak et al., 2005). Cysteine-rich EPIDERMAL PATTERNING FACTOR peptides (EPFs) bind to the ectodomains of ER, ERL1 and ERL2 which form constitutive complexes with the ectodomain of the receptor-like protein (RLP) TOO MANY MOUTH (TMM) Vl and elution at 0.75 ml min -1 was monitored by ultraviolet absorbance at λ = 280 nm. To chimera; # numbers indicate independent lines.(C) Anti-GFP western blot together with the Ponceau-stained membrane as loading control.

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“…) and CIK co‐receptors (Hu et al . ), the second through the receptor‐like protein CLAVATA2 (CLV2; Kayes & Clark ) that acts in complex with the pseudokinase CORYNE (CRN; Müller et al . ).…”

Section: Post‐translationally Modified Peptides and Peptide Familiesmentioning

confidence: 99%

Regulation of plant peptide hormones and growth factors by post‐translational modification

Stührwohldt

Schaller

2018

Plant Biol J

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The number, diversity and significance of peptides as regulators of cellular differentiation, growth, development and defence of plants has long been underestimated. Peptides have now emerged as an important class of signals for cell-to-cell communication over short distances, and also for long-range signalling. We refer to these signalling molecules as peptide growth factors and peptide hormones, respectively. As compared to remarkable progress with respect to the mechanisms of peptide perception and signal transduction, the biogenesis of signalling peptides is still in its infancy. This review focuses on the biogenesis and activity of small post-translationally modified peptides. These peptides are derived from inactive pre-pro-peptides of approximately 70-120 amino acids. Multiple post-translational modifications (PTMs) may be required for peptide maturation and activation, including proteolytic processing, tyrosine sulfation, proline hydroxylation and hydroxyproline glycosylation. While many of the enzymes responsible for these modifications have been identified, their impact on peptide activity and signalling is not fully understood. These PTMs may or may not be required for bioactivity, they may inactivate the peptide or modify its signalling specificity, they may affect peptide stability or targeting, or its binding affinity with the receptor. In the present review, we will first introduce the peptides that undergo PTMs and for which these PTMs were shown to be functionally relevant. We will then discuss the different types of PTMs and the impact they have on peptide activity and plant growth and development. We conclude with an outlook on the open questions that need to be addressed in future research.

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A group of receptor kinases are essential for CLAVATA signalling to maintain stem cell homeostasis

Cited by 156 publications

References 31 publications

CLE25 peptide regulates phloem initiation in Arabidopsis through a CLERK‐CLV2 receptor complex

CLE25 peptide regulates phloem initiation in Arabidopsis through a CLERK‐CLV2 receptor complex

Constitutive activation of leucine-rich repeat receptor kinase signaling pathways by BAK1-interacting receptor-like kinase 3 chimera

Regulation of plant peptide hormones and growth factors by post‐translational modification

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