In vitro characterization of the homogalacturonan-binding domain of the wall-associated kinase WAK1 using site-directed mutagenesis

Decreux, Annabelle; Thomas, A. G.; Spies, B; Brasseur, Robert; Cutsem, Pierre Van; Messiaen, Johan

doi:10.1016/j.phytochem.2006.03.009

Cited by 100 publications

(90 citation statements)

References 45 publications

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“…Mutations in the WAK2cTAP extracellular domain that eliminate pectin binding also suppressed the phenotype (21), and the results reported here indicate that the activating pectin needs to be de-esterified. This is in agreement with the in vitro binding activities of WAK1 and -2, which have a higher binding of de-esterified over esterified pectins in vitro (25,26).…”

Section: Discussionsupporting

confidence: 89%

“…Due to this overlapping expression and tight linkage, it has been hard to distinguish their respective contributions to pectin sensing (18). In vitro, WAK1 and WAK2 bind to long pectin chains reflective of a native pectin form (homogalacturonan) but have a preference for short OGs of degree of polymerization 9 -15 (17,25,26). De-esterified pectins have a much higher binding to WAK1 than do esterified pectins (25).…”

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confidence: 99%

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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

Kohorn

Saba

et al. 2014

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 89%

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confidence: 99%

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

Saba

et al. 2014

Journal of Biological Chemistry

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“…The extracellular non-EGF domain of WAK1 and WAK2 was shown to bind to pectin in vitro and this is enhanced by a calcium-induced bridging of the pectin (Decreux and Messiaen 2005;Decreux et al 2006). Also, it has been shown that the assembly and crosslinking of WAKs may begin at an early stage within a cytoplasmic compartment rather than in the cell wall itself, and is coordinated with synthesis of surface cellulose (Kohorn et al 2006b).…”

Section: Functional Studies Of Different Wak Members Inmentioning

confidence: 99%

RNAi mediated silencing of a wall associated kinase, OsiWAK1 in Oryza sativa results in impaired root development and sterility due to anther indehiscence

Kanneganti

Gupta

2011

Physiol Mol Biol Plants

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The Wall-Associated Kinase, one of the receptorlike kinase (RLK) gene families in plant, plays important roles in cell expansion, pathogen resistance and heavy metal stress tolerance in Arabidopsis thaliana. Here, we isolated a cDNA encoding a novel WAK from indica rice and designated as OsiWAK1 (Oryza sativa indica WAK-1). In this study, the RNAi construct with OsiWAK1 gene cloned in sense and antisense orientation separated by a functional intron under constitutive promoter, was introduced through biolistic gene gun method into the rice cultivar "IR-50" to determine the effect of OsiWAK1 transcript silencing on rice plant development. Examination of the transgenic plants reveals that OsiWAK1 transcript silencing in rice results in dwarf plants because of the reduction in the size of leaves, flag-leaves, internodes and panicle. The development of root primordia during germination, root hairs and lateral rooting was also effected. Microscopic analysis revealed that the decrease in size is due to reduction in the cell size but not the number of cells. In addition, the transgenic plants also exhibited sterile phenotype due to anther indehiscence and 40 % reduction in pollen viability. These data suggest that OsiWAK1 may play an important role in rice plant growth and development.

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“…WAKs display the typical eukaryotic Ser/Thr kinase signature and an extracytoplasmic domain (ectodomain) containing several EGF-like repeats. WAK1 and WAK2 bind in vitro to OGs and pectin through the N-terminal non-EGF portion of the ectodomain (15,17,18). Moreover, WAK2 has been recently shown to be required for the activation by pectin of numerous genes in protoplasts, including that encoding a vacuolar invertase (18).…”

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confidence: 99%

A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides

Brutus

Sicilia

Macone

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

636

540

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Oligogalacturonides (OGs) released from the plant cell wall are active both as damage-associated molecular patterns (DAMPs) for the activation of the plant immune response and regulators of plant growth and development. Members of the Wall-Associated Kinase (WAK) family are candidate receptors of OGs, due to their ability to bind in vitro these oligosaccharides. Because lethality and redundancy have hampered the study of WAKs by reverse genetics, we have adopted a chimeric receptor approach to elucidate the role of Arabidopsis WAK1. In a test-of-concept study, we first defined the appropriate chimera design and demonstrated that the Arabidopsis pattern recognition receptor (PRR) EFR is amenable to the construction of functional and resistanceconferring chimeric receptors carrying the ectodomain of another Arabidopsis PRR, FLS2. After, we analyzed chimeras derived from EFR and WAK1. Our results show that, upon stimulation with OGs, the WAK1 ectodomain is capable of activating the EFR kinase domain. On the other hand, upon stimulation with the cognate ligand elf18, the EFR ectodomain activates the WAK1 kinase, triggering defense responses that mirror those normally activated by OGs and are effective against fungal and bacterial pathogens. Finally, we show that transgenic plants overexpressing WAK1 are more resistant to Botrytis cinerea.damage-associated molecular patterns | elongation factor tu receptor | pectin-mediated signaling | plant immunity | chimeric receptors

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In vitro characterization of the homogalacturonan-binding domain of the wall-associated kinase WAK1 using site-directed mutagenesis

Cited by 100 publications

References 45 publications

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

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

RNAi mediated silencing of a wall associated kinase, OsiWAK1 in Oryza sativa results in impaired root development and sterility due to anther indehiscence

A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides

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