BRI1 controls vascular cell fate in the
            <i>Arabidopsis</i>
            root through RLP44 and phytosulfokine signaling

Holzwart, Eleonore; Huerta, Apolonio Ignacio; Glöckner, Nina; Gómez, Borja Garnelo; Wanke, Friederike; Augustin, Sebastian; Askani, Jana Christin; Schürholz, Ann-Kathrin; Harter, Klaus; Wolf, Sebastián

doi:10.1073/pnas.1814434115

Cited by 81 publications

(151 citation statements)

References 71 publications

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“…Interference with HG de-methylesterification triggers BR signaling: overexpression of a PME inhibitor protein or exposing plants to epigallocatechin gallate (EGCG), a chemical that inhibits PME activity, impairs directional organ growth, a phenotype caused by an activation of BR signaling (Wolf et al, 2012b). RECEPTOR-LIKE PROTEIN44 (RLP44) interacts with the BR receptor BRASSINOSTEROID INSENSITIVE1 (BRI1) and the co-receptor BRI1-ASSOCIATED RECEPTOR KINASE (BAK1), likely acting as a scaffold to increase the association between BRI1 and BAK1 (Wolf et al, 2014;Holzwart et al, 2018). RLP44 is also essential for BR-mediated response to altered HG demethylesterification (Wolf et al, 2014).…”

Section: Downstream Signaling Eventsmentioning

confidence: 99%

A wall with integrity: surveillance and maintenance of the plant cell wall under stress

2019

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Summary The structural and functional integrity of the cell wall needs to be constantly monitored and fine‐tuned to allow for growth while preventing mechanical failure. Many studies have advanced our understanding of the pathways that contribute to cell wall biosynthesis and how these pathways are regulated by external and internal cues. Recent evidence also supports a model in which certain aspects of the wall itself may act as growth‐regulating signals. Molecular components of the signaling pathways that sense and maintain cell wall integrity have begun to be revealed, including signals arising in the wall, sensors that detect changes at the cell surface, and downstream signal transduction modules. Abiotic and biotic stress conditions provide new contexts for the study of cell wall integrity, but the nature and consequences of wall disruptions due to various stressors require further investigation. A deeper understanding of cell wall signaling will provide insights into the growth regulatory mechanisms that allow plants to survive in changing environments.

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Section: Downstream Signaling Eventsmentioning

confidence: 99%

A wall with integrity: surveillance and maintenance of the plant cell wall under stress

2019

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“…To decipher the contribution of individual putative phosphorylation sites to RLP44 function, we mutated each of the sites individually to alanine in RLP44-GFP and quantified the capacity of these constructs to complement cnu2. We reasoned that working with near endogenous expression levels might increase the sensitivity of the complementation assay, therefore all RLP44-GFP variants were driven by the RLP44 promoter (Holzwart et al, 2018b). To assess comparability between the previously characterized overexpression lines, we also generated RLP44 promoter-driven Pdead and Pmimic versions, in which all four putative phosphosites are mutated as previously described.…”

Section: Phosphorylation At Individual Sites Has Opposing Effects On mentioning

confidence: 99%

“…Basic fuchsin staining of five-day-old seedling roots and CLSM analysis was performed as described (Holzwart et al, 2018b).…”

Section: Xylem Cell Number Analysismentioning

confidence: 99%

Phosphorylation-dependent routing of RLP44 towards brassinosteroid or phytosulfokine signalling

Gómez

Lozano‐Durán

Wolf

2019

Preprint

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Plants rely on a complex network of cell surface receptors to integrate developmental and environmental cues into behaviour adapted to the conditions. The largest group of these receptors, leucine-rich repeat receptor-like kinases, form a complex interaction network that is modulated and extended by receptor-like proteins. This raises the question of how specific outputs can be generated when receptor proteins are engaged in a plethora of promiscuous interactions. RECEPTOR-LIKE PROTEIN 44 acts to promote brassinosteroid and phytosulfokine signalling, which orchestrate a wide variety of cellular responses. However, it is unclear how these activities are coordinated. Here, we show that RLP44 is phosphorylated in its highly conserved C-terminal cytosolic tail and that this post-translational modification governs its subcellular localization. RLP44 variants in which phosphorylation is blocked enter endocytosis prematurely, leading to an almost entirely intracellular localization, whereas mimicking phosphorylation results in preferential RLP44 localization at the plasma membrane. Phosphorylation is crucial for regulating RLP44's interaction with the brassinosteroid receptor BRASSINOSTEROID INSENSITIVE 1, and thus its function in BR signalling activation. In contrast, the interaction of RLP44 with PHYTOSULFOKINE RECEPTOR 1 is not affected by its phospho-status. Analysis of the contribution of individual amino acid modifications suggests that routing of RLP44 to its target receptor complexes is controlled by its phosphorylation pattern, providing a framework to understand how a common component of different receptor complexes can get specifically engaged in a particular signalling pathway.

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“…The RECEPTOR-LIKE PROTEIN 44 (RLP44) was previously described to play a role in cell wall integrity sensing via modulation of brassinosteroid-mediated responses (Wolf et al, 2014). It directly interacts with both BRI1 and BAK1 (Wolf et al, 2014;Holzwart et al, 2018) (Holzwart et al, 2019). A recent study also showed that RLP44 plays a role in vascular development, which involves phytosulfokine hormone signalling (Holzwart et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

“…It directly interacts with both BRI1 and BAK1 (Wolf et al, 2014;Holzwart et al, 2018) (Holzwart et al, 2019). A recent study also showed that RLP44 plays a role in vascular development, which involves phytosulfokine hormone signalling (Holzwart et al, 2018). The phospho-state of the short, C-terminal tail of RLP44 is important for the interaction with BRI1 and determines, whether RLP44 is located at the PM or internalized into intracellular compartments (Garnelo Gomez et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Three-fluorophore FRET enables the analysis of ternary protein association in living plant cells

Glöckner

Oven-Krockhaus

Rohr

et al. 2019

Preprint

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Integration of signalling on the cellular level is essential for the survival of organisms.Protein-protein interaction studies provide valuable insights in these signalling events.One of the best understood signalling pathways in plants is the brassinosteroid (BR) hormone signalling pathway, which is mediated by the receptor BRASSINOSTEROID INSENSITIVE 1 (BRI1) with its co-receptor BRI1-ASSOCIATED KINASE (BAK1). Both BRI1 and BAK1 have been shown to interact with RECEPTOR LIKE PROTEIN 44 (RLP44), which was implicated in cell wall integrity sensing by modulation of BL signalling. Here we provide evidence by quantitative in vivo three-fluorophore FRET-FLIM measurements, that RLP44, BRI1 and BAK1 form a trimeric complex in the plasma membrane of N. benthamiana leaf cells, with an estimated distance between them below 15 nm. The immune receptor FLAGELLIN SENSING 2 (FLS2), which is also a receptor-like kinase like BRI1, is not integrated in a similar complex with RLP44 and BAK1. Our study supports that BRI1 and FLS2 are localized in distinct nanodomains in the PM. As the fluorescence lifetime of the donor is monitored, our method circumvents the extensive calculations necessitated by intensity-based FRET interaction assays and thus provides a feasible base for studying the sub-compartmentalization in the plasma membrane of living plant cells with a nanoscale resolution.

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BRI1 controls vascular cell fate in the Arabidopsis root through RLP44 and phytosulfokine signaling

Cited by 81 publications

References 71 publications

A wall with integrity: surveillance and maintenance of the plant cell wall under stress

A wall with integrity: surveillance and maintenance of the plant cell wall under stress

Phosphorylation-dependent routing of RLP44 towards brassinosteroid or phytosulfokine signalling

Three-fluorophore FRET enables the analysis of ternary protein association in living plant cells

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