Wolf, Sebastian, van der Does, Dieuwertje, Ladwig, Friederike, Sticht, Carsten, Kolbeck, Andreas, Schürholz, Ann-Kathrin, Augustin, Sebastian, Keinath, Nana, Rausch, Thomas, Greiner, Steffen, Schumacher, Karin, Harter, Klaus, Zipfel, Cyril and Höfte, Herman (2014) A receptor-like protein mediates the response to pectin modification by activating brassinosteroid signaling. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 111 (42). pp. 15261-6. ISSN 1091-6490
Full text not available from this repository.Abstract
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.
Item Type: | Article |
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Uncontrolled Keywords: | 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 |
Faculty \ School: | Faculty of Science > School of Biological Sciences |
UEA Research Groups: | Faculty of Science > Research Groups > Plant Sciences |
Depositing User: | Pure Connector |
Date Deposited: | 09 Mar 2016 14:00 |
Last Modified: | 21 Oct 2022 04:33 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/57393 |
DOI: | 10.1073/pnas.1322979111 |
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