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An oomycete effector co-opts a host RabGAP protein to remodel pathogen interface and subvert defense-related secretion
Open accessPreprint — published as 10.1126/sciadv.ado9516
Abstract
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), TBC1D15L, to remodel the host-pathogen interface. The effector, PiE354, hijacks TBC1D15L as a susceptibility factor to usurp its GAP activity on Rab8a—a key Rab GTPase crucial for defense-related secretion. By hijacking TBC1D15L, 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.
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Metadata
- Authors
- Yuen, E. L. H., Tumtas, Y., Chan, L. I., Ibrahim, T., Evangelisti, E., Tulin, F., Skłenar, J., Menke, F., Kamoun, S., Bubeck, D., Schornack, S., & Bozkurt, T. O.
- Affiliations
- Imperial College London (GB)
- Carnegie Institution for Science (US)
- University of East Anglia (GB)
- University of Cambridge (GB)
- Corresponding author
- Schornack, Sebastian
- Bozkurt, Tolga O.
- ORCID
- Venue
- Science Advances
- Publisher
- openRxiv
- Published
- 2024-01-15
- Volume
- 10
- Issue
- 40
- Pages
- eado9516-eado9516
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC11451530
- OpenAlex
- W4403114824
- Cited by
- 19
- References
- 1
- Citations by year
- 2026: 13 · 2025: 4 · 2024: 1
- FWCI
- 4.37
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Science Advances (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UEA Digital Repository (University of East Anglia) (acceptedVersion)
- Spiral (Imperial College London) (submittedVersion, cc-by)
- Funders
- University of East Anglia
- Imperial College London
- Biotechnology and Biological Sciences Research Council (BB/K018639/1, BB/V002937/1, 1654544, BB/M022315/1, BBS/E/JI/230001B, BB/F021216/1, BB/W008157/1, BBS/E/J/000PR9798, BBS/E/J/000PR9797, BB/L018535/1, BB/X511055/1, BB/X016382/1, BB/W002221/1, BB/T017929/1, BBS/E/JI/230001D, BB/I020470/1, BBS/E/J/000PR9795, BB/T006102/1, BBS/E/JI/230001A, BBS/E/J/000CA523)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Pathogens and Resistance
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Disease Resistance and Genetics
- Keywords
- plant pathogenic oomycetes, effector proteins, Rab8a, host-pathogen interface, membrane trafficking
- MeSH terms
- Cell Membrane, Oomycetes, Plant Diseases, Arabidopsis, GTPase-Activating Proteins, rab GTP-Binding Proteins, Host-Pathogen Interactions
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