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Flavonol-induced changes in PIN2 polarity and auxin transport in the Arabidopsis thaliana rol1-2 mutant require phosphatase activity
BM. Kuhn, T. Nodzyński, S. Errafi, R. Bucher, S. Gupta, B. Aryal, P. Dobrev, L. Bigler, M. Geisler, E. Zažímalová, J. Friml, C. Ringli,
Language English Country England, Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
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PubMed
28165500
DOI
10.1038/srep41906
Knihovny.cz E-resources
- MeSH
- Arabidopsis drug effects genetics metabolism MeSH
- Flavonoids pharmacology MeSH
- Glucosyltransferases genetics metabolism MeSH
- Indoleacetic Acids metabolism MeSH
- Mutation MeSH
- Protein Phosphatase 2 genetics metabolism MeSH
- Arabidopsis Proteins genetics metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
The phytohormone auxin is a major determinant and regulatory component important for plant development. Auxin transport between cells is mediated by a complex system of transporters such as AUX1/LAX, PIN, and ABCB proteins, and their localization and activity is thought to be influenced by phosphatases and kinases. Flavonols have been shown to alter auxin transport activity and changes in flavonol accumulation in the Arabidopsis thaliana rol1-2 mutant cause defects in auxin transport and seedling development. A new mutation in ROOTS CURL IN NPA 1 (RCN1), encoding a regulatory subunit of the phosphatase PP2A, was found to suppress the growth defects of rol1-2 without changing the flavonol content. rol1-2 rcn1-3 double mutants show wild type-like auxin transport activity while levels of free auxin are not affected by rcn1-3. In the rol1-2 mutant, PIN2 shows a flavonol-induced basal-to-apical shift in polar localization which is reversed in the rol1-2 rcn1-3 to basal localization. In vivo analysis of PINOID action, a kinase known to influence PIN protein localization in a PP2A-antagonistic manner, revealed a negative impact of flavonols on PINOID activity. Together, these data suggest that flavonols affect auxin transport by modifying the antagonistic kinase/phosphatase equilibrium.
Department of Biology geislerLab University of Fribourg Fribourg Switzerland
Institute of Chemistry University of Zurich Zurich Switzerland
Institute of Experimental Botany Academy of Sciences of the Czech Republic Prague Czech Republic
Institute of Plant and Microbial Biology University of Zurich Zurich Switzerland
Institute of Science and Technology Austria Am Campus 1 3400 Klosterneuburg Austria
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