Tomato Pistil Factor STIG1 Promotes in Vivo Pollen Tube Growth by Binding to Phosphatidylinositol 3-Phosphate and the Extracellular Domain of the Pollen Receptor Kinase LePRK2

Huang, Weijie; Liu, Haikuan; McCormick, Susan P.; Tang, Weihua

doi:10.1105/tpc.114.123281

Cited by 69 publications

(46 citation statements)

References 63 publications

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“…A leucine-rich repeat RLK mediates GRI-peptide-induced ion leakage GRI is related to the Solanaceae stigma-specific protein STIG1 (Goldman et al, 1994). Tomato LeSTIG1 interacted in vitro with the ectodomains of two RLKs, the pollen receptor kinases LePRK1 and LePRK2 (Tang et al, 2004;Löcke et al, 2010;Huang et al, 2014). Therefore, we tested the potential interaction of GRI with RLKs.…”

Section: Resultsmentioning

confidence: 99%

GRIM REAPER peptide binds to receptor kinase PRK 5 to trigger cell death in Arabidopsis

et al. 2014

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Recognition of extracellular peptides by plasma membranelocalized receptor proteins is commonly used in signal transduction. In plants, very little is known about how extracellular peptides are processed and activated in order to allow recognition by receptors. Here, we show that induction of cell death in planta by a secreted plant protein GRIM REAPER (GRI) is dependent on the activity of the type II metacaspase METACASPASE-9. GRI is cleaved by METACASPASE-9 in vitro resulting in the release of an 11 amino acid peptide. This peptide bound in vivo to the extracellular domain of the plasma membrane-localized, atypical leucine-rich repeat receptorlike kinase POLLEN-SPECIFIC RECEPTOR-LIKE KINASE 5 (PRK5) and was sufficient to induce oxidative stress/ROS-dependent cell death. This shows a signaling pathway in plants from processing and activation of an extracellular protein to recognition by its receptor.

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Section: Resultsmentioning

confidence: 99%

GRIM REAPER peptide binds to receptor kinase PRK 5 to trigger cell death in Arabidopsis

et al. 2014

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“…So far, most identified ligands for functionally studied LRR-RLKs are small molecules and oligopeptides (Fletcher et al, 1999;Wang et al, 2001;Matsubayashi et al, 2002;Tang et al, 2002;Caño-Delgado et al, 2004;Kinoshita et al, 2005;Ito et al, 2006;Kondo et al, 2006;Stenvik et al, 2008;Shimada et al, 2011;Lee et al, 2012;Torii, 2012;Butenko et al, 2014;Huang et al, 2014;Matsubayashi, 2014). Although using similar coreceptors/partners, BRI1-SERK1, FLS2-BAK1, and EMS1-SERK1 are activated by different types of ligands.…”

Section: Discussionmentioning

confidence: 99%

Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination

Wang

Huang

et al. 2016

Plant Physiol.

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Cell signaling pathways mediated by leucine-rich repeat receptor-like kinases (LRR-RLKs) are essential for plant growth, development, and defense. The EMS1 (EXCESS MICROSPOROCYTES1) LRR-RLK and its small protein ligand TPD1 (TAPETUM DETERMINANT1) play a fundamental role in somatic and reproductive cell differentiation during early anther development in Arabidopsis (Arabidopsis thaliana). However, it is unclear whether other cell surface molecules serve as coregulators of EMS1. Here, we show that SERK1 (SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1) and SERK2 LRR-RLKs act redundantly as coregulatory and physical partners of EMS1. The SERK1/2 genes function in the same genetic pathway as EMS1 in anther development. Bimolecular fluorescence complementation, Förster resonance energy transfer, and coimmunoprecipitation approaches revealed that SERK1 interacted biochemically with EMS1. Transphosphorylation of EMS1 by SERK1 enhances EMS1 kinase activity. Among 12 in vitro autophosphorylation and transphosphorylation sites identified by tandem mass spectrometry, seven of them were found to be critical for EMS1 autophosphorylation activity. Furthermore, complementation test results suggest that phosphorylation of EMS1 is required for its function in anther development. Collectively, these data provide genetic and biochemical evidence of the interaction and phosphorylation between SERK1/2 and EMS1 in anther development.

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“…These kinases interact with KINASE PARTNER PROTEIN (KPP) (Kaothien et al, 2005), a RopGEF that activates a tomato ROP in vitro (Löcke et al, 2010). LePRK2 is a positive regulator of pollen tube growth (Zhang et al, 2008), as antisense LePRK2 pollen tubes grow slower and exhibit an attenuated response to the growth-promoting signals STYLE INTERACTOR FOR LePRKs (STIL) (Wengier et al, 2010) and STIGMA-SPECIFIC PROTEIN1 (Huang et al, 2014). Furthermore, the phosphorylation status of particular motifs in the juxtamembrane domain of LePRK2 reciprocally affected pollen tube growth rate (Salem et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Overexpression of the Tomato Pollen Receptor Kinase LePRK1 Rewires Pollen Tube Growth to a Blebbing Mode

Gui¹,

Dong²,

Liu³

et al. 2014

The Plant Cell

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Tomato Pistil Factor STIG1 Promotes in Vivo Pollen Tube Growth by Binding to Phosphatidylinositol 3-Phosphate and the Extracellular Domain of the Pollen Receptor Kinase LePRK2

Cited by 69 publications

References 63 publications

GRIM REAPER peptide binds to receptor kinase PRK 5 to trigger cell death in Arabidopsis

GRIM REAPER peptide binds to receptor kinase PRK 5 to trigger cell death in Arabidopsis

Two SERK Receptor-Like Kinases Interact with EMS1 to Control Anther Cell Fate Determination

Overexpression of the Tomato Pollen Receptor Kinase LePRK1 Rewires Pollen Tube Growth to a Blebbing Mode

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