Requirement for Pectin Methyl Esterase and Preference for Fragmented over Native Pectins for Wall-associated Kinase-activated, EDS1/PAD4-dependent Stress Response in Arabidopsis

Kohorn, Bruce D.; Kohorn, Susan L.; Saba, N.; Meco, Victoriano

doi:10.1074/jbc.m114.567545

Cited by 70 publications

(63 citation statements)

References 33 publications

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“…The response is dependent upon MPK6 and the pathogen response transcription factors EDS1 and PAD4. Importantly, the WAK2 cTAP allele is also suppressed by a null allele of a pectin methyl esterase, pme3 (33). This provides genetic evidence that WAKs are sensing the de-esterified form of pectin, consistent with the higher affinity in vitro of WAKs for de-esterified over esterified pectin and for pectin fragments of limited degrees of polymerization, 9 -15 sugars (30,31,35,36).…”

supporting

confidence: 51%

“…This provides genetic evidence that WAKs are sensing the de-esterified form of pectin, consistent with the higher affinity in vitro of WAKs for de-esterified over esterified pectin and for pectin fragments of limited degrees of polymerization, 9 -15 sugars (30,31,35,36). The pme3/pme3 mutant plant is more responsive to OGs than WT plants, as measured by the induction of the FADLox gene, a robust marker for OG induction of transcription (29,33,34). The data support a model in which OGs are competing with native pectin to bind WAKs, thus providing a mechanism for WAKs to distinguish changes in the pectin network and activate alternate pathways.…”

mentioning

confidence: 56%

“…A dominant WAK2 allele WAK2 cTAP , whose encoded protein requires a functional pectin-binding domain and an active kinase, induces a constitutive stress response (33,34). The response is dependent upon MPK6 and the pathogen response transcription factors EDS1 and PAD4.…”

mentioning

confidence: 99%

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Rapid Oligo-Galacturonide Induced Changes in Protein Phosphorylation in Arabidopsis

Kohorn

Hoon

Minkoff

et al. 2016

Molecular & Cellular Proteomics

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The wall-associated kinases (WAKs) 1 are receptor protein kinases that bind to long polymers of cross-linked pectin in the cell wall. These plasma-membrane-associated protein kinases also bind soluble pectin fragments called oligo-galacturonides (OGs) released from the wall after pathogen attack and damage. WAKs are required for cell expansion during development but bind water soluble OGs generated from walls with a higher affinity than the wall-associated polysaccharides. OGs activate a WAKdependent, distinct stress-like response pathway to help plants resist pathogen attack. In this report, a quantitative mass-spectrometric-based phosphoproteomic analysis was used to identify Arabidopsis cellular events rapidly induced by OGs in planta. Using N 14/ N 15 isotopic in vivo metabolic labeling, we screened 1,000 phosphoproteins for rapid OG-induced changes and found 50 proteins with increased phosphorylation, while there were none that decreased significantly. Seven of the phosphosites within these proteins overlap with those altered by another signaling molecule plants use to indicate the presence of pathogens (the bacterial "elicitor" peptide Flg22), indicating distinct but overlapping pathways activated by these two types of chemicals. Genetic analysis of genes encoding 10 OG-specific and two Flg22/OG-induced phosphoproteins reveals that null mutations in eight proteins compromise the OG response. These phosphorylated proteins with genetic evidence supporting their role in the OG response include two cytoplasmic kinases, two membrane-associated scaffold proteins, a phospholipase C, a CDPK, an unknown cadmium response protein, and a motor protein. The cell walls of angiosperms are composed of a complex arrangement of cellulose, hemicellulose, and pectin and are assembled through a complex, developmentally regulated coordination of synthesis, turnover, and interactions between protein and carbohydrates (1). The pectins can be selectively and locally cross-linked into a structural network that is subsequently remodeled and degraded by enzymes, and these events have dramatic effects on cell enlargement (2-6). Pathogens and mechanical disruptions also cause fragmentation and, thus, release of the pectin, leading often to a plant stress response (7-9).A number of receptor kinases such as THE1, FER, HERK, ANX, and RLP44 have been termed cell wall sensors (10 -18) and typically have extracellular domains containing leucinerich regions and a malectin carbohydrate-binding domain, although an experimentally demonstrated role for polysaccharide binding to their extracellular domains is unclear. Of the plant putative "wall sensors" only the wall-associated kinases (WAKs) are known to bind to a cell wall component, pectin, and these are distinguished also by their unique extracellular domain that lacks leucine-rich repeats and contains instead epidermal growth factor (EGF) repeats as well as a pectin-binding region (19).Pectins are synthesized in the Golgi apparatus as methyl esterified 1-4 D-galacturonic acids and are secret...

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supporting

confidence: 51%

mentioning

confidence: 56%

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Rapid Oligo-Galacturonide Induced Changes in Protein Phosphorylation in Arabidopsis

Kohorn

Hoon

Minkoff

et al. 2016

Molecular & Cellular Proteomics

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“…OGs used for experiments described in Figures 8 to 10 and Supplemental Figure 12 were a kind gift from Simone Ferrari. OGs used in experiments described in Figure 13 and Supplemental Figures 11, 13, and 15 were prepared as previously described (Kohorn et al, 2014).…”

Section: Treatment With Macerozyme or Ogsmentioning

confidence: 99%

Pectin Biosynthesis Is Critical for Cell Wall Integrity and Immunity in Arabidopsis thaliana

et al. 2016

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(D.J.K.); 0000-0001-5167-736X (J.G.)Plant cell walls are important barriers against microbial pathogens. Cell walls of Arabidopsis thaliana leaves contain three major types of polysaccharides: cellulose, various hemicelluloses, and pectins. UDP-D-galacturonic acid, the key building block of pectins, is produced from the precursor UDP-D-glucuronic acid by the action of glucuronate 4-epimerases (GAEs). Pseudomonas syringae pv maculicola ES4326 (Pma ES4326) repressed expression of GAE1 and GAE6 in Arabidopsis, and immunity to Pma ES4326 was compromised in gae6 and gae1 gae6 mutant plants. These plants had brittle leaves and cell walls of leaves had less galacturonic acid. Resistance to specific Botrytis cinerea isolates was also compromised in gae1 gae6 double mutant plants. Although oligogalacturonide (OG)-induced immune signaling was unaltered in gae1 gae6 mutant plants, immune signaling induced by a commercial pectinase, macerozyme, was reduced. Macerozyme treatment or infection with B. cinerea released less soluble uronic acid, likely reflecting fewer OGs, from gae1 gae6 cell walls than from wild-type Col-0. Although both OGs and macerozyme-induced immunity to B. cinerea in Col-0, only OGs also induced immunity in gae1 gae6. Pectin is thus an important contributor to plant immunity, and this is due at least in part to the induction of immune responses by soluble pectin, likely OGs, that are released during plant-pathogen interactions.

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“…(FADLox), a gene known to be responsive to pectins (Denoux et al, 2008;Kohorn et al, 2014). The expression level of FADLox was ∼5-fold higher in qua2-1 than in the wild type, qua2-1/esmd1-1 and esmd1-1 (Fig.…”

Section: A Constitutive Pectin-related Signaling Is Associated With Tmentioning

confidence: 99%

Cell adhesion in plants is under the control of putative O-fucosyltransferases

Verger¹,

Chabout²,

Gineau³

et al. 2016

Journal of Cell Science

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Cell-to-cell adhesion in plants is mediated by the cell wall and the presence of a pectin-rich middle lamella. However, we know very little about how the plant actually controls and maintains cell adhesion during growth and development and how it deals with the dynamic cell wall remodeling that takes place. Here we investigate the molecular mechanisms that control cell adhesion in plants. We carried out a genetic suppressor screen and a genetic analysis of cell adhesion-defective Arabidopsis thaliana mutants. We identified a genetic suppressor of a cell adhesion defect affecting a putative O-fucosyltransferase. Furthermore, we show that the state of cell adhesion is not directly linked with pectin content in the cell wall but instead is associated with altered pectin-related signaling. Our results suggest that cell adhesion is under the control of a feedback signal from the state of the pectin in the cell wall. Such a mechanism could be necessary for the control and maintenance of cell adhesion during growth and development.

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Requirement for Pectin Methyl Esterase and Preference for Fragmented over Native Pectins for Wall-associated Kinase-activated, EDS1/PAD4-dependent Stress Response in Arabidopsis

Cited by 70 publications

References 33 publications

Rapid Oligo-Galacturonide Induced Changes in Protein Phosphorylation in Arabidopsis

Rapid Oligo-Galacturonide Induced Changes in Protein Phosphorylation in Arabidopsis

Pectin Biosynthesis Is Critical for Cell Wall Integrity and Immunity in Arabidopsis thaliana

Cell adhesion in plants is under the control of putative O-fucosyltransferases

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