Pectin methylesterase activity is required for RALF1 peptide signalling output

Author:

Rößling Ann-Kathrin12,Dünser Kai13,Liu Chenlu12,Lauw Susan45,Rodriguez-Franco Marta1,Kalmbach Lothar1,Barbez Elke12,Kleine-Vehn Jürgen123

Affiliation:

1. Institute of Biology II

2. Center for Integrative Biological Signalling Studies (CIBSS), University of Freiburg

3. Institute of Molecular Plant Biology (IMPB), Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences (BOKU)

4. University of Freiburg

5. Centre for Biological Signalling Studies (BIOSS), University of Freiburg

Abstract

The extracellular matrix plays an integrative role in cellular responses in plants, but its contribution to the signalling of extracellular ligands largely remains to be explored. RAPID ALKALINIZATION FACTORs (RALFs) are extracellular peptide hormones that play pivotal roles in various physiological processes. Here, we address a crucial connection between the de-methylesterification machinery of the cell wall component pectin and RALF1 activity. Pectin is a polysaccharide, contributing to the structural integrity of the cell wall. Our data illustrate that the pharmacological and genetic interference with PECTIN METHYL ESTERASEs (PMEs) abolishes RALF1-induced root growth repression. Our data suggest that positively charged RALF1 peptides bind negatively charged, de-methylesterified pectin with high avidity. We illustrate that the RALF1 association with de-methylesterified pectin is required for its FERONIA-dependent perception, contributing to the control of the extracellular matrix and the regulation of plasma membrane dynamics. Notably, this mode of action is independent of the FER-dependent extracellular matrix sensing mechanism provided by FER interaction with the Leucine-Rich Repeat Extensin (LRX) proteins. We propose that the methylation status of pectin acts as a contextualizing signalling scaffold for RALF peptides, linking extracellular matrix dynamics to peptide hormone-mediated responses.

Publisher

eLife Sciences Publications, Ltd

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