Title: Effects of Arabidopsis wall associated kinase mutations on ESMERALDA1 and elicitor induced ROS
Angiosperm cell adhesion is dependent on interactions between pectin polysaccharides which make up a significant portion of the plant cell wall. Cell adhesion in Arabidopsis may also be regulated through a pectin-related signaling cascade mediated by a putative O-fucosyltransferase ESMERALDA1 (ESMD1), and the Epidermal Growth Factor (EGF) domains of the pectin binding Wall associated Kinases (WAKs) are a primary candidate substrate for ESMD1 activity. Genetic interactions between WAKs and ESMD1 were examined using a dominant hyperactive allele of WAK2, WAK2cTAP , and a mutant of the putative O-fucosyltransferase ESMD1. WAK2cTAP expression results in a dwarf phenotype and activation of the stress response and reactive oxygen species (ROS) production, while esmd1 is a suppressor of a pectin deficiency induced loss of adhesion. Here we find that esmd1 suppresses the WAK2cTAP dwarf and stress response phenotype, including ROS accumulation and gene expression. Additional analysis suggests that mutations of the potential WAK EGF O-fucosylation site also abate the WAK2cTAP phenotype, yet only evidence for an N-linked but not O-linked sugar addition can be found. Moreover, a WAK locus deletion allele has no effect on the ability of esmd1 to suppress an adhesion deficiency, indicating WAKs and their modification are not a required component of the potential ESMD1 signaling mechanism involved in the control of cell adhesion. The WAK locus deletion does however affect the induction of ROS but not the transcriptional response induced by the elicitors Flagellin, Chitin and oligogalacturonides (OGs). more »« less
Kohorn, Bruce D.; Dexter-Meldrum, Jacob; Zorensky, Frances D.; Chabout, Salem; Mouille, Gregory; Kohorn, Susan
(, Plants)
null
(Ed.)
The cellulose- and pectin-rich plant cell wall defines cell structure, mediates defense against pathogens, and facilitates plant cell adhesion. An adhesion mutant screen of Arabidopsis hypocotyls identified a new allele of QUASIMODO2 (QUA2), a gene required for pectin accumulation and whose mutants have reduced pectin content and adhesion defects. A suppressor of qua2 was also isolated and describes a null allele of SABRE (SAB), which encodes a previously described plasma membrane protein required for longitudinal cellular expansion that organizes the tubulin cytoskeleton. sab mutants have increased pectin content, increased levels of expression of pectin methylesterases and extensins, and reduced cell surface area relative to qua2 and Wild Type, contributing to a restoration of cell adhesion.
Edwards, Harley; Zavorskas, Joseph; Huso, Walker; Doan, Alexander G; Grey, Kelsey; Lee, JungHun; Morse, Meredith; Wilkinson, Heather H; Ebbole, Danniel; Shaw, Brian D; et al
(, bioRxiv)
Abstract Under synchronized conidiation, over 2500 gene products show differential expression, including transcripts for bothbrlAandabaA, which increase steadily over time. In contrast, during wall-stress induced by the echinocandin micafungin, thebrlAtranscript is upregulated while theabaAtranscript is not. In addition, whenmpkA(last protein kinase in the cell wall integrity signaling pathway) is deleted,brlAexpression is not upregulated in response to wall stress. Together, these data imply BrlA may play a role in a cellular stress-response which is independent of the canonical BrlA-mediated conidiation pathway. To test this hypothesis, we performed a genome-wide search and found 332 genes with a putative BrlA response element (BRE) in their promoter region. From this set, we identified 28 genes which were differentially expressed in response to wall-stress, but not during synchronized conidiation. This set included seven gene products whose homologues are involved in transmembrane transport and 14 likely to be involved in secondary metabolite biosynthesis. We selected six of these genes for further examination and find that they all show altered expression behavior in thebrlAdeletion strain. Together, these data support the idea that BrlA plays a role in various biological processes outside asexual development. ImportanceTheAspergillus nidulanstranscription factor BrlA is widely accepted as a master regulator of conidiation. Here, we show that in addition to this function BrlA appears to play a role in responding to cell-wall stress. We note that this has not been observed outsideA. nidulans. Further, BrlA-mediated conidiation is highly conserved acrossAspergillusspecies, so this new functionality is likely relevant in otherAspergilli. We identified several transmembrane transporters that have altered transcriptional responses to cell-wall stress in abrlAdeletion mutant. Based on our observation, together with what is known about thebrlAgene locus’ regulation, we identifybrlAβas the likely intermediary in function ofbrlAin the response to cell-wall stress.
Kohorn, Bruce D.; Zorensky, Frances D.; Dexter-Meldrum, Jacob; Chabout, Salem; Mouille, Gregory; Kohorn, Susan
(, Development)
null
(Ed.)
ABSTRACT Plant growth, morphogenesis and development involve cellular adhesion, a process dependent on the composition and structure of the extracellular matrix or cell wall. Pectin in the cell wall is thought to play an essential role in adhesion, and its modification and cleavage are suggested to be highly regulated so as to change adhesive properties. To increase our understanding of plant cell adhesion, a population of ethyl methanesulfonate-mutagenized Arabidopsis were screened for hypocotyl adhesion defects using the pectin binding dye Ruthenium Red that penetrates defective but not wild-type (WT) hypocotyl cell walls. Genomic sequencing was used to identify a mutant allele of ELMO1 which encodes a 20 kDa Golgi membrane protein that has no predicted enzymatic domains. ELMO1 colocalizes with several Golgi markers and elmo1−/− plants can be rescued by an ELMO1-GFP fusion. elmo1−/− exhibits reduced mannose content relative to WT but no other cell wall changes and can be rescued to WT phenotype by mutants in ESMERALDA1, which also suppresses other adhesion mutants. elmo1 describes a previously unidentified role for the ELMO1 protein in plant cell adhesion.
Fichman, Yosef; Zandalinas, Sara I.; Peck, Scott; Luan, Sheng; Mittler, Ron
(, The Plant Cell)
Abstract Reactive oxygen species (ROS), produced by respiratory burst oxidase homologs (RBOHs) at the apoplast, play a key role in local and systemic cell-to-cell signaling, required for plant acclimation to stress. Here we reveal that the Arabidopsis thaliana leucine-rich-repeat receptor-like kinase H2O2-INDUCED CA2+ INCREASES 1 (HPCA1) acts as a central ROS receptor required for the propagation of cell-to-cell ROS signals, systemic signaling in response to different biotic and abiotic stresses, stress responses at the local and systemic tissues, and plant acclimation to stress, following a local treatment of high light (HL) stress. We further report that HPCA1 is required for systemic calcium signals, but not systemic membrane depolarization responses, and identify the calcium-permeable channel MECHANOSENSITIVE ION CHANNEL LIKE 3, CALCINEURIN B-LIKE CALCIUM SENSOR 4 (CBL4), CBL4-INTERACTING PROTEIN KINASE 26 and Sucrose-non-fermenting-1-related Protein Kinase 2.6/OPEN STOMATA 1 (OST1) as required for the propagation of cell-to-cell ROS signals. In addition, we identify serine residues S343 and S347 of RBOHD (the putative targets of OST1) as playing a key role in cell-to-cell ROS signaling in response to a local application of HL stress. Our findings reveal that HPCA1 plays a key role in mediating and coordinating systemic cell-to-cell ROS and calcium signals required for plant acclimation to stress.
In deciphering the global signaling capacity of FERONIA receptor kinase, Liu, Yeh, et al. discovered an extracellular phase separation process driven by FERONIA peptide ligand RALF-cell wall polysaccharide pectin interaction, which leads to cognate and non-cognate receptor clustering and promiscuous endocytosis as a coping mechanism in response to environmental stressors. Highlights Cell surface pectin-RALF1 phase separation recruits FERONIA-LLG1 into condensates RALF induces FERONIA-LLG1-dependent promiscuous receptor clustering and endocytosis RALF1-pectin molecular condensates function as surface sensors for stress signals FERONIA-LLG1-mediated global endocytosis ensures plant resilience under stress
Kohorn, Bruce D., Greed, Bridgid E., Mouille, Gregory, Verger, Stéphane, and Kohorn, Susan L. Effects of Arabidopsis wall associated kinase mutations on ESMERALDA1 and elicitor induced ROS. Retrieved from https://par.nsf.gov/biblio/10249749. PLOS ONE 16.5 Web. doi:10.1371/journal.pone.0251922.
Kohorn, Bruce D., Greed, Bridgid E., Mouille, Gregory, Verger, Stéphane, & Kohorn, Susan L. Effects of Arabidopsis wall associated kinase mutations on ESMERALDA1 and elicitor induced ROS. PLOS ONE, 16 (5). Retrieved from https://par.nsf.gov/biblio/10249749. https://doi.org/10.1371/journal.pone.0251922
Kohorn, Bruce D., Greed, Bridgid E., Mouille, Gregory, Verger, Stéphane, and Kohorn, Susan L.
"Effects of Arabidopsis wall associated kinase mutations on ESMERALDA1 and elicitor induced ROS". PLOS ONE 16 (5). Country unknown/Code not available. https://doi.org/10.1371/journal.pone.0251922.https://par.nsf.gov/biblio/10249749.
@article{osti_10249749,
place = {Country unknown/Code not available},
title = {Effects of Arabidopsis wall associated kinase mutations on ESMERALDA1 and elicitor induced ROS},
url = {https://par.nsf.gov/biblio/10249749},
DOI = {10.1371/journal.pone.0251922},
abstractNote = {Angiosperm cell adhesion is dependent on interactions between pectin polysaccharides which make up a significant portion of the plant cell wall. Cell adhesion in Arabidopsis may also be regulated through a pectin-related signaling cascade mediated by a putative O-fucosyltransferase ESMERALDA1 (ESMD1), and the Epidermal Growth Factor (EGF) domains of the pectin binding Wall associated Kinases (WAKs) are a primary candidate substrate for ESMD1 activity. Genetic interactions between WAKs and ESMD1 were examined using a dominant hyperactive allele of WAK2, WAK2cTAP , and a mutant of the putative O-fucosyltransferase ESMD1. WAK2cTAP expression results in a dwarf phenotype and activation of the stress response and reactive oxygen species (ROS) production, while esmd1 is a suppressor of a pectin deficiency induced loss of adhesion. Here we find that esmd1 suppresses the WAK2cTAP dwarf and stress response phenotype, including ROS accumulation and gene expression. Additional analysis suggests that mutations of the potential WAK EGF O-fucosylation site also abate the WAK2cTAP phenotype, yet only evidence for an N-linked but not O-linked sugar addition can be found. Moreover, a WAK locus deletion allele has no effect on the ability of esmd1 to suppress an adhesion deficiency, indicating WAKs and their modification are not a required component of the potential ESMD1 signaling mechanism involved in the control of cell adhesion. The WAK locus deletion does however affect the induction of ROS but not the transcriptional response induced by the elicitors Flagellin, Chitin and oligogalacturonides (OGs).},
journal = {PLOS ONE},
volume = {16},
number = {5},
author = {Kohorn, Bruce D. and Greed, Bridgid E. and Mouille, Gregory and Verger, Stéphane and Kohorn, Susan L.},
editor = {Zabotina, Olga A.}
}
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