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Yuen, Enoch Lok Him, Tumtas, Yasin, King, Freddie, Ibrahim, Tarhan, Chan, Lok I., Evangelisti, Edouard, Tulin, Frej, Skłenar, Jan, Menke, Frank L. H. 
ORCID: https://orcid.org/0000-0003-2490-4824, Kamoun, Sophien ORCID: https://orcid.org/0000-0002-0290-0315, Bubeck, Doryen, Schornack, Sebastian and Bozkurt, Tolga Osman
(2024)
A pathogen effector co-opts a host RabGAP protein to remodel pathogen interface and subvert defense-related secretion.
Science Advances, 10 (40).
ISSN 2375-2548
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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), 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.
| Item Type: | Article |
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| Additional Information: | Data and materials availability: All data needed to evaluate the conclusions in the paper are present in the paper and/or the Supplementary Materials. AF2-M predictions are uploaded to the public repository figshare and are available at https://doi.org/10.6084/m9.figshare.24846558. The constructs generated by the Schornack lab can be provided by S.S. pending a completed material transfer agreement. Requests for these materials should be submitted to sebastian.schornack@slcu.cam.ac.uk. Funding information: E.L.H.Y. is funded by BBSRC grants (BB/X511055/1) and (BB/X016382/1). Y.T. and T.O.B. are funded by BBSRC grant (BB/T006102/1). T.I. is funded by BBSRC grant (BB/X511055/1). E.E. and F.T. are funded by European Research Council (ERC-2014-STG, H2020, and 637537). S.S. is funded by Gatsby Foundation (GAT3395/GLD) and Royal Society (RG69135). |
| Faculty \ School: | Faculty of Science > The Sainsbury Laboratory Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Plant Sciences |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 24 Oct 2024 16:30 |
| Last Modified: | 09 Nov 2024 00:54 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/97187 |
| DOI: | 10.1126/sciadv.ado9516 |
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