A receptor-like protein mediates the response to pectin modification by activating brassinosteroid signaling

Sebastian Wolf, Dieuwertje van der Does, Friederike Ladwig, Carsten Sticht, Andreas Kolbeck, Ann-Kathrin Schürholz, Sebastian Augustin, Nana Keinath, Thomas Rausch, Steffen Greiner, Karin Schumacher, Klaus Harter, Cyril Zipfel, Herman Höfte

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118 Citations (Scopus)


The brassinosteroid (BR) signaling module is a central regulator of plant morphogenesis, as indicated by the large number of BR-responsive cell wall-related genes and the severe growth defects of BR mutants. Despite a detailed knowledge of the signaling components, the logic of this auto-/paracrine signaling module in growth control remains poorly understood. Recently, extensive cross-talk with other signaling pathways has been shown, suggesting that the outputs of BR signaling, such as gene-expression changes, are subject to complex control mechanisms. We previously provided evidence for a role of BR signaling in a feedback loop controlling the integrity of the cell wall. Here, we identify the first dedicated component of this feedback loop: a receptor-like protein (RLP44), which is essential for the compensatory triggering of BR signaling upon inhibition of pectin de-methylesterification in the cell wall. RLP44 is required for normal growth and stress responses and connects with the BR signaling pathway, presumably through a direct interaction with the regulatory receptor-like kinase BAK1. These findings corroborate a role for BR in controlling the sensitivity of a feedback signaling module involved in maintaining the physico-chemical homeostasis of the cell wall during cell expansion.

Original languageEnglish
Pages (from-to)15261-6
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America (PNAS)
Issue number42
Publication statusPublished - 21 Oct 2014


  • Arabidopsis Proteins
  • Brassinosteroids
  • Cell Wall
  • Cloning, Molecular
  • Gene Expression Profiling
  • Gene Expression Regulation, Plant
  • Homeostasis
  • Ligands
  • Microscopy, Confocal
  • Mutation
  • Pectins
  • Phenotype
  • Plant Proteins
  • Protein Binding
  • Protein Interaction Mapping
  • Protein-Serine-Threonine Kinases
  • Signal Transduction

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