Dynamic localization of a helper NLR at the plant–pathogen interface underpins pathogen recognition
| Autor: | Cian Duggan, Chih-Hang Wu, Abbas Maqbool, Toby Ross Martin, Zachary Savage, Hiroaki Adachi, Yasin Tumtas, Eleonora Moratto, Tolga O. Bozkurt, Sophien Kamoun, Stephen Rothery, Eranthika Hamilton, Seda Nohut, Alexandre Y Leary |
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| Přispěvatelé: | Biotechnology and Biological Sciences Research Council (BBSRC) |
| Rok vydání: | 2021 |
| Předmět: |
Phytophthora infestans
Mutant NLR Proteins Biology helper NLR Immune system Haustorium Tobacco cell biology Plant Immunity Receptors Immunologic Extrahaustorial membrane Receptor Pathogen Disease Resistance Plant Diseases Plant Proteins Multidisciplinary Effector Cell Membrane Biological Sciences Subcellular localization Cell biology plant disease resistance Host-Pathogen Interactions host–microbe interactions |
| Zdroj: | Proc Natl Acad Sci U S A |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.2104997118 |
| Popis: | Plants employ sensor-helper pairs of NLR immune receptors to recognize pathogen effectors and activate immune responses (1). Yet the subcellular localization of NLRs pre- and post-activation during pathogen infection remains poorly understood. Here we show that NRC4, from the ‘NRC’ solanaceous helper NLR family (1), undergoes dynamic changes in subcellular localization by shuttling to and from the plant-pathogen haustorium interface established during infection by the Irish potato famine pathogen Phytophthora infestans. Specifically, prior to activation, NRC4 accumulates at the extra-haustorial membrane (EHM), presumably to mediate response to perihaustorial effectors, that are recognized by NRC4- dependent sensor NLRs. However not all NLRs accumulate at the EHM, as the closely related helper NRC2, and the distantly related ZAR1, did not accumulate at the EHM. NRC4 required an intact N-terminal coiled coil domain to accumulate at the EHM, whereas the functionally conserved MADA motif implicated in cell death activation and membrane insertion was dispensable for this process. Strikingly, a constitutively autoactive NRC4 mutant did not accumulate at the EHM and showed punctate distribution that mainly associated with the plasma membrane, suggesting that post-activation, NRC4 may undergo a conformation switch to form clusters that do not preferentially associate with the EHM. When NRC4 is activated by a sensor NLR during infection however, NRC4 forms puncta mainly at the EHM and to a lesser extent at the plasma membrane. We conclude that following activation at the EHM, NRC4 may spread to other cellular membranes from its primary site of activation to trigger immune responses. |
| Databáze: | OpenAIRE |
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