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Xanthomonas effector XopR hijacks host actin cytoskeleton via complex coacervation

Author

Listed:
  • He Sun

    (Nanyang Technological University)

  • Xinlu Zhu

    (Nanyang Technological University)

  • Chuanxi Li

    (Nanyang Technological University)

  • Zhiming Ma

    (Nanyang Technological University)

  • Xiao Han

    (Nanyang Technological University)

  • Yuanyuan Luo

    (Nanyang Technological University)

  • Liang Yang

    (Nanyang Technological University
    Nanyang Technological University)

  • Jing Yu

    (Nanyang Technological University)

  • Yansong Miao

    (Nanyang Technological University)

Abstract

The intrinsically disordered region (IDR) is a preserved signature of phytobacterial type III effectors (T3Es). The T3E IDR is thought to mediate unfolding during translocation into the host cell and to avoid host defense by sequence diversification. Here, we demonstrate a mechanism of host subversion via the T3E IDR. We report that the Xanthomonas campestris T3E XopR undergoes liquid-liquid phase separation (LLPS) via multivalent IDR-mediated interactions that hijack the Arabidopsis actin cytoskeleton. XopR is gradually translocated into host cells during infection and forms a macromolecular complex with actin-binding proteins at the cell cortex. By tuning the physical-chemical properties of XopR-complex coacervates, XopR progressively manipulates multiple steps of actin assembly, including formin-mediated nucleation, crosslinking of F-actin, and actin depolymerization, which occurs through competition for actin-depolymerizing factor and depends on constituent stoichiometry. Our findings unravel a sophisticated strategy in which bacterial T3E subverts the host actin cytoskeleton via protein complex coacervation.

Suggested Citation

  • He Sun & Xinlu Zhu & Chuanxi Li & Zhiming Ma & Xiao Han & Yuanyuan Luo & Liang Yang & Jing Yu & Yansong Miao, 2021. "Xanthomonas effector XopR hijacks host actin cytoskeleton via complex coacervation," Nature Communications, Nature, vol. 12(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24375-3
    DOI: 10.1038/s41467-021-24375-3
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    Cited by:

    1. Ziwei Zhu & Jun Xiong & Hao Shi & Yuchen Liu & Junjie Yin & Kaiwei He & Tianyu Zhou & Liting Xu & Xiaobo Zhu & Xiang Lu & Yongyan Tang & Li Song & Qingqing Hou & Qing Xiong & Long Wang & Daihua Ye & T, 2023. "Magnaporthe oryzae effector MoSPAB1 directly activates rice Bsr-d1 expression to facilitate pathogenesis," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Aravind Chandrasekaran & Kristin Graham & Jeanne C. Stachowiak & Padmini Rangamani, 2024. "Kinetic trapping organizes actin filaments within liquid-like protein droplets," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Qianqian Ma & Wahyu Surya & Danxia He & Hanmeng Yang & Xiao Han & Mui Hoon Nai & Chwee Teck Lim & Jaume Torres & Yansong Miao, 2024. "Spa2 remodels ADP-actin via molecular condensation under glucose starvation," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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