TY - GEN A1 - Albers, Philip A1 - Uestuen, Suayib A1 - Witzel, Katja A1 - Bornke, Frederik T1 - Identification of a novel target of the bacterial effector HopZ1a T2 - Phytopathology N2 - The plant pathogen Pseudomonas syringae is a gram-negative bacterium which infects a wide range of plant species including important crops plants. To suppress plant immunity and cause disease P.syringae injects type-III effector proteins (T3Es) into the plant cell cytosol. In this study, we identified a novel target of the well characterized bacterial T3E HopZ1a. HopZ1a is an acetyltransferase that was shown to disrupt vesicle transport during innate immunity by acetylating tubulin. Using a yeast-two-hybrid screen approach, we identified a REMORIN (REM) protein from tobacco as a novel HopZ1a target. HopZ1a interacts with REM at the plasma membrane (PM) as shown by split-YFP experiments. Interestingly, we found that PBS1, a well-known kinase involved in plant immunity also interacts with REM in pull-down assays, and at the PM as shown by BiFC. Furthermore, we confirmed that REM is phosphorylated by PBS1 in vitro. Overexpression of REM provokes the upregulation of defense genes and leads to disease-like phenotypes pointing to a role of REM in plant immune signaling. Further protein-protein interaction studies reveal novel REM binding partners with a possible role in plant immune signaling. Thus, REM might act as an assembly hub for an immune signaling complex targeted by HopZ1a. Taken together, this is the first report describing that a REM protein is targeted by a bacterial effector. How HopZ1a might mechanistically manipulate the plant immune system through interfering with REM function will be discussed. Y1 - 2018 SN - 0031-949X SN - 1943-7684 VL - 108 IS - 10 PB - American Phytopathological Society CY - Saint Paul ER - TY - JOUR A1 - Uestuen, Suayib A1 - Börnke, Frederik T1 - Interactions of Xanthomonas type-III effector proteins with the plant ubiquitin and ubiquitin-like pathways JF - Frontiers in plant science N2 - In eukaryotes, regulated protein turnover is required during many cellular processes, including defense against pathogens. Ubiquitination and degradation of ubiquitinated proteins via the ubiquitin proteasome system (UPS) is the main pathway for the turnover of intracellular proteins in eukaryotes. The extensive utilization of the UPS in host cells makes it an ideal pivot for the manipulation of cellular processes by pathogens. Like many other Gram-negative bacteria, Xanthomonas species secrete a suite of type-III effector proteins (T3Es) into their host cells to promote virulence. Some of these T3Es exploit the plant UPS to interfere with immunity. This review summarizes T3E examples from the genus Xanthomonas with a proven or suggested interaction with the host UPS or UPS-like systems and also discusses the apparent paradox that arises from the presence of T3Es that inhibit the UPS in general while others rely on its activity for their function. KW - Xanthomonas KW - type-III effector KW - ubiquitin KW - proteasome KW - plant defense Y1 - 2014 U6 - https://doi.org/10.3389/fpls.2014.00736 SN - 1664-462X VL - 5 PB - Frontiers Research Foundation CY - Lausanne ER - TY - JOUR A1 - Leong, Jia Xuan A1 - Raffeiner, Margot A1 - Spinti, Daniela A1 - Langin, Gautier A1 - Franz-Wachtel, Mirita A1 - Guzman, Andrew R. A1 - Kim, Jung-Gun A1 - Pandey, Pooja A1 - Minina, Alyona E. A1 - Macek, Boris A1 - Hafren, Anders A1 - Bozkurt, Tolga O. A1 - Mudgett, Mary Beth A1 - Börnke, Frederik A1 - Hofius, Daniel A1 - Uestuen, Suayib T1 - A bacterial effector counteracts host autophagy by promoting degradation of an autophagy component JF - The EMBO journal N2 - Beyond its role in cellular homeostasis, autophagy plays anti- and promicrobial roles in host-microbe interactions, both in animals and plants. One prominent role of antimicrobial autophagy is to degrade intracellular pathogens or microbial molecules, in a process termed xenophagy. Consequently, microbes evolved mechanisms to hijack or modulate autophagy to escape elimination. Although well-described in animals, the extent to which xenophagy contributes to plant-bacteria interactions remains unknown. Here, we provide evidence that Xanthomonas campestris pv. vesicatoria (Xcv) suppresses host autophagy by utilizing type-III effector XopL. XopL interacts with and degrades the autophagy component SH3P2 via its E3 ligase activity to promote infection. Intriguingly, XopL is targeted for degradation by defense-related selective autophagy mediated by NBR1/Joka2, revealing a complex antagonistic interplay between XopL and the host autophagy machinery. Our results implicate plant antimicrobial autophagy in the depletion of a bacterial virulence factor and unravel an unprecedented pathogen strategy to counteract defense-related autophagy in plant-bacteria interactions. KW - autophagy KW - effectors KW - immunity KW - ubiquitination KW - xenophagy Y1 - 2022 U6 - https://doi.org/10.15252/embj.2021110352 SN - 1460-2075 VL - 41 IS - 13 PB - Wiley CY - Hoboken ER -