| Autor: |
Yuen ELH; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK., Tumtas Y; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK., King F; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK., Ibrahim T; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK., Chan LI; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK., Evangelisti E; Sainsbury Laboratory (SLCU), University of Cambridge, Cambridge CB2 1LR, UK.; Université Côte d'Azur, INRAE UMR 1355, CNRS UMR 7254, Institut Sophia Agrobiotech (ISA), 06903 Sophia Antipolis, France., Tulin F; Sainsbury Laboratory (SLCU), University of Cambridge, Cambridge CB2 1LR, UK.; Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA., Skłenar J; The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK., Menke FLH; The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK., Kamoun S; The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK., Bubeck D; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK., Schornack S; Sainsbury Laboratory (SLCU), University of Cambridge, Cambridge CB2 1LR, UK., Bozkurt TO; Department of Life Sciences, Imperial College London, London SW7 2AZ, UK. |
| Abstrakt: |
Pathogens have evolved sophisticated mechanisms to manipulate host cell membrane dynamics, a crucial adaptation to survive in hostile environments shaped by innate immune responses. Plant-derived membrane interfaces, engulfing invasive hyphal projections of fungal and oomycete pathogens, are prominent junctures dictating infection outcomes. Understanding how pathogens transform these host-pathogen interfaces to their advantage remains a key biological question. Here, we identified a conserved effector, secreted by plant pathogenic oomycetes, that co-opts a host Rab GTPase-activating protein (RabGAP), TOPGAP, to remodel the host-pathogen interface. The effector, PiE354, hijacks TOPGAP as a susceptibility factor to usurp its GAP activity on Rab8a, a key Rab GTPase crucial for defense-related secretion. By hijacking TOPGAP, PiE354 purges Rab8a from the plasma membrane, diverting Rab8a-mediated immune trafficking away from the pathogen interface. This mechanism signifies an uncanny evolutionary adaptation of a pathogen effector in co-opting a host regulatory component to subvert defense-related secretion, thereby providing unprecedented mechanistic insights into the reprogramming of host membrane dynamics by pathogens. |
