1. Department of Plant Microbe Interactions, Max-Planck-Institut für Züchtungsforschung, Carl-von-Linné-Weg 10, D-50829 Köln, Germany
2. ZMBP, Plant Biochemistry, Eberhard-Karls-Universität Tübingen, Auf der Morgenstelle 5, D-72076 Tübingen, Germany
3. ZMBP, Developmental Genetics, Eberhard-Karls-Universität Tübingen, Auf der Morgenstelle 3, D-72076 Tübingen, Germany
4. Present addresses: Sainsbury Laboratory, John Innes Centre, Norwich, Norfolk NR4 7UH, UK (U.L. and V.L.); Institut für Biologie II, Universität Freiburg, Sonnenstrasse 5, D-79104 Freiburg, Germany (C.N.).

Correspondence to: Ralph Panstruga¹Volker Lipka^1,2,4Paul Schulze-Lefert¹ Correspondence and requests for materials should be addressed to V.L. (Email: Volker.Lipka@sainsbury-laboratory.ac.uk), R.P. (Email: panstrug@mpiz-koeln.mpg.de) or P.S.-L. (Email: schlef@mpiz-koeln.mpg.de).

Abstract

Cell-autonomous immunity is widespread in plant–fungus interactions and terminates fungal pathogenesis either at the cell surface or after pathogen entry. Although post-invasive resistance responses typically coincide with a self-contained cell death of plant cells undergoing attack by parasites, these cells survive pre-invasive defence. Mutational analysis in Arabidopsis identified PEN1 syntaxin as one component of two pre-invasive resistance pathways against ascomycete powdery mildew fungi^{1, 2, 3}. Here we show that plasma-membrane-resident PEN1 promiscuously forms SDS-resistant soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) complexes together with the SNAP33 adaptor and a subset of vesicle-associated membrane proteins (VAMPs). PEN1-dependent disease resistance acts in vivo mainly through two functionally redundant VAMP72 subfamily members, VAMP721 and VAMP722. Unexpectedly, the same two VAMP proteins also operate redundantly in a default secretory pathway, suggesting dual functions in separate biological processes owing to evolutionary co-option of the default pathway for plant immunity. The disease resistance function of the secretory PEN1–SNAP33–VAMP721/722 complex and the pathogen-induced subcellular dynamics of its components are mechanistically reminiscent of immunological synapse formation in vertebrates, enabling execution of immune responses through focal secretion.

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