Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 117, Issue 17, Pages 9621-9629Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1907799117
Keywords
membrane domain; receptor signaling; plasmodesmata; immunity
Categories
Funding
- Biotechnology and Biological Research Council [BB/L000466/1, BBS/E/J/000PR9796]
- European Research Council [725459, 309858]
- Japan Society for the Promotion of Science KAKENHI [JP16H06186, JP16KT0037]
- John Innes Foundation
- Gatsby Charitable Foundation
- European Research Council (ERC) [725459, 309858] Funding Source: European Research Council (ERC)
- BBSRC [BBS/E/J/000PR9796, BB/L000466/1] Funding Source: UKRI
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The plasma membrane (PM) is composed of heterogeneous sub-domains, characterized by differences in protein and lipid composition. PM receptors can be dynamically sorted into membrane domains to underpin signaling in response to extracellular stimuli. In plants, the plasmodesmal PM is a discrete microdomain that hosts specific receptors and responses. We exploited the independence of this PM domain to investigate how membrane domains can independently integrate a signal that triggers responses across the cell. Focusing on chitin signaling, we found that responses in the plasmodesmal PM require the LysM receptor kinases LYK4 and LYK5 in addition to LYM2. Chitin induces dynamic changes in the localization, association, or mobility of these receptors, but only LYM2 and LYK4 are detected in the plasmodesmal PM. We further uncovered that chitin-induced production of reactive oxygen species and callose depends on specific signaling events that lead to plasmodesmata closure. Our results demonstrate that distinct membrane domains can integrate a common signal with specific machinery that initiates discrete signaling cascades to produce a localized response.
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