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The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate immune responses.
New Phytol. 2014 Jul; 203(2):592-606.NP

Abstract

Mitogen-activated protein kinase (MAPK) cascades play key roles in plant immune signalling, and elucidating their regulatory functions requires the identification of the pathway-specific substrates. We used yeast two-hybrid interaction screens, in vitro kinase assays and mass spectrometry-based phosphosite mapping to study a family of MAPK substrates. Site-directed mutagenesis and promoter-reporter fusion studies were performed to evaluate the impact of substrate phosphorylation on downstream signalling. A subset of the Arabidopsis thaliana VQ-motif-containing proteins (VQPs) were phosphorylated by the MAPKs MPK3 and MPK6, and renamed MPK3/6-targeted VQPs (MVQs). When plant protoplasts (expressing these MVQs) were treated with the flagellin-derived peptide flg22, several MVQs were destabilized in vivo. The MVQs interact with specific WRKY transcription factors. Detailed analysis of a representative member of the MVQ subset, MVQ1, indicated a negative role in WRKY-mediated defence gene expression - with mutation of the VQ-motif abrogating WRKY binding and causing mis-regulation of defence gene expression. We postulate the existence of a variety of WRKY-VQP-containing transcriptional regulatory protein complexes that depend on spatio-temporal VQP and WRKY expression patterns. Defence gene transcription can be modulated by changing the composition of these complexes - in part - through MAPK-mediated VQP degradation.

Authors+Show Affiliations

Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120, Halle, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

24750137

Citation

Pecher, Pascal, et al. "The Arabidopsis Thaliana Mitogen-activated Protein Kinases MPK3 and MPK6 Target a Subclass of 'VQ-motif'-containing Proteins to Regulate Immune Responses." The New Phytologist, vol. 203, no. 2, 2014, pp. 592-606.
Pecher P, Eschen-Lippold L, Herklotz S, et al. The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate immune responses. New Phytol. 2014;203(2):592-606.
Pecher, P., Eschen-Lippold, L., Herklotz, S., Kuhle, K., Naumann, K., Bethke, G., Uhrig, J., Weyhe, M., Scheel, D., & Lee, J. (2014). The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate immune responses. The New Phytologist, 203(2), 592-606. https://doi.org/10.1111/nph.12817
Pecher P, et al. The Arabidopsis Thaliana Mitogen-activated Protein Kinases MPK3 and MPK6 Target a Subclass of 'VQ-motif'-containing Proteins to Regulate Immune Responses. New Phytol. 2014;203(2):592-606. PubMed PMID: 24750137.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate immune responses. AU - Pecher,Pascal, AU - Eschen-Lippold,Lennart, AU - Herklotz,Siska, AU - Kuhle,Katja, AU - Naumann,Kai, AU - Bethke,Gerit, AU - Uhrig,Joachim, AU - Weyhe,Martin, AU - Scheel,Dierk, AU - Lee,Justin, Y1 - 2014/04/22/ PY - 2014/01/16/received PY - 2014/03/18/accepted PY - 2014/4/23/entrez PY - 2014/4/23/pubmed PY - 2015/5/15/medline KW - VQ-motif KW - defence KW - immunity KW - mitogen-activated protein kinase (MAPK) KW - pathogen-associated molecular pattern (PAMP) KW - phosphorylation KW - signalling SP - 592 EP - 606 JF - The New phytologist JO - New Phytol. VL - 203 IS - 2 N2 - Mitogen-activated protein kinase (MAPK) cascades play key roles in plant immune signalling, and elucidating their regulatory functions requires the identification of the pathway-specific substrates. We used yeast two-hybrid interaction screens, in vitro kinase assays and mass spectrometry-based phosphosite mapping to study a family of MAPK substrates. Site-directed mutagenesis and promoter-reporter fusion studies were performed to evaluate the impact of substrate phosphorylation on downstream signalling. A subset of the Arabidopsis thaliana VQ-motif-containing proteins (VQPs) were phosphorylated by the MAPKs MPK3 and MPK6, and renamed MPK3/6-targeted VQPs (MVQs). When plant protoplasts (expressing these MVQs) were treated with the flagellin-derived peptide flg22, several MVQs were destabilized in vivo. The MVQs interact with specific WRKY transcription factors. Detailed analysis of a representative member of the MVQ subset, MVQ1, indicated a negative role in WRKY-mediated defence gene expression - with mutation of the VQ-motif abrogating WRKY binding and causing mis-regulation of defence gene expression. We postulate the existence of a variety of WRKY-VQP-containing transcriptional regulatory protein complexes that depend on spatio-temporal VQP and WRKY expression patterns. Defence gene transcription can be modulated by changing the composition of these complexes - in part - through MAPK-mediated VQP degradation. SN - 1469-8137 UR - https://www.unboundmedicine.com/medline/citation/24750137/The_Arabidopsis_thaliana_mitogen_activated_protein_kinases_MPK3_and_MPK6_target_a_subclass_of_'VQ_motif'_containing_proteins_to_regulate_immune_responses_ L2 - https://doi.org/10.1111/nph.12817 DB - PRIME DP - Unbound Medicine ER -