@article{ShubchynskyyBonieckaSchweighoferetal.2017,
  author    = {Shubchynskyy, Volodymyr and Boniecka, Justyna and Schweighofer, Alois and Simulis, Justinas and Kvederaviciute, Kotryna and Stumpe, Michael and Mauch, Felix and Balazadeh, Salma and M{\"u}ller-R{\"o}ber, Bernd and Boutrot, Freddy and Zipfel, Cyril and Meskiene, Irute},
  title     = {Protein phosphatase AP2C1 negatively regulates basal resistance and defense responses to Pseudomonas syringae},
  series = {Journal of experimental botany},
  volume    = {68},
  journal   = {Journal of experimental botany},
  number    = {5},
  publisher = {Oxford Univ. Press},
  address   = {Oxford},
  issn      = {0022-0957},
  doi       = {10.1093/jxb/erw485},
  pages     = {1169 -- 1183},
  year      = {2017},
  abstract  = {Mitogen-activated protein kinases (MAPKs) mediate plant immune responses to pathogenic bacteria. However, less is known about the cell autonomous negative regulatory mechanism controlling basal plant immunity. We report the biological role of Arabidopsis thaliana MAPK phosphatase AP2C1 as a negative regulator of plant basal resistance and defense responses to Pseudomonas syringae. AP2C2, a closely related MAPK phosphatase, also negatively controls plant resistance. Loss of AP2C1 leads to enhanced pathogen-induced MAPK activities, increased callose deposition in response to pathogen-associated molecular patterns or to P. syringae pv. tomato (Pto) DC3000, and enhanced resistance to bacterial infection with Pto. We also reveal the impact of AP2C1 on the global transcriptional reprogramming of transcription factors during Pto infection. Importantly, ap2c1 plants show salicylic acid-independent transcriptional reprogramming of several defense genes and enhanced ethylene production in response to Pto. This study pinpoints the specificity of MAPK regulation by the different MAPK phosphatases AP2C1 and MKP1, which control the same MAPK substrates, nevertheless leading to different downstream events. We suggest that precise and specific control of defined MAPKs by MAPK phosphatases during plant challenge with pathogenic bacteria can strongly influence plant resistance.},
  language  = {en}
}
@article{AlbersUestuenWitzeletal.2019,
  author    = {Albers, Philip and {\"U}st{\"u}n, Suayib and Witzel, Katja and Kraner, Max Erdmund and B{\"o}rnke, Frederik},
  title     = {A Remorin from Nicotiana benthamiana Interacts with the Pseudomonas Type-III Effector Protein HopZ1a and is Phosphorylated by the Immune-Related Kinase PBS1},
  series = {Molecular Plant-Microbe Interactions},
  volume    = {32},
  journal   = {Molecular Plant-Microbe Interactions},
  number    = {9},
  publisher = {Amer phytopathological SOC},
  address   = {ST Paul},
  issn      = {0894-0282},
  doi       = {10.1094/MPMI-04-19-0105-R},
  pages     = {1229 -- 1242},
  year      = {2019},
  abstract  = {The plasma membrane (PM) is at the interface of plant-pathogen interactions and, thus, many bacterial type-III effector (T3E) proteins target membrane-associated processes to interfere with immunity. The Pseudomonas syringae T3E HopZ1a is a host cell PM-localized effector protein that has several immunity-associated host targets but also activates effector-triggered immunity in resistant backgrounds. Although HopZ1a has been shown to interfere with early defense signaling at the PM, no dedicated PM-associated HopZ1a target protein has been identified until now. Here, we show that HopZ1a interacts with the PM-associated remorin protein NbREM4 from Nicotiana benthamiana in several independent assays. NbREM4 relocalizes to membrane nanodomains after treatment with the bacterial elicitor flg22 and transient overexpression of NbREM4 in N. benthamiana induces the expression of a subset of defense-related genes. We can further show that NbREM4 interacts with the immune-related receptor-like cytoplasmic kinase avrPphB-susceptible 1 (PBS1) and is phosphorylated by PBS1 on several residues in vitro. Thus, we conclude that NbREM4 is associated with early defense signaling at the PM. The possible relevance of the HopZ1a-NbREM4 interaction for HopZ1a virulence and avirulence functions is discussed.},
  language  = {en}
}