@article{JarickBertscheStahletal.2018,
  author    = {Jarick, Marcel and Bertsche, Ute and Stahl, Mark and Schultz, Daniel and Methling, Karen and Lalk, Michael and Stigloher, Christian and Steger, Mirco and Schlosser, Andreas and Ohlsen, Knut},
  title     = {The serine/threonine kinase Stk and the phosphatase Stp regulate cell wall synthesis in Staphylococcus aureus},
  series = {Scientific Reports},
  volume    = {8},
  journal   = {Scientific Reports},
  number    = {13693},
  doi       = {10.1038/s41598-018-32109-7},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-177333},
  year      = {2018},
  abstract  = {The cell wall synthesis pathway producing peptidoglycan is a highly coordinated and tightly regulated process. Although the major components of bacterial cell walls have been known for decades, the complex regulatory network controlling peptidoglycan synthesis and many details of the cell division machinery are not well understood. The eukaryotic-like serine/threonine kinase Stk and the cognate phosphatase Stp play an important role in cell wall biosynthesis and drug resistance in S. aureus. We show that stp deletion has a pronounced impact on cell wall synthesis. Deletion of stp leads to a thicker cell wall and decreases susceptibility to lysostaphin. Stationary phase Δstp cells accumulate peptidoglycan precursors and incorporate higher amounts of incomplete muropeptides with non-glycine, monoglycine and monoalanine interpeptide bridges into the cell wall. In line with this cell wall phenotype, we demonstrate that the lipid II:glycine glycyltransferase FemX can be phosphorylated by the Ser/Thr kinase Stk in vitro. Mass spectrometric analyses identify Thr32, Thr36 and Ser415 as phosphoacceptors. The cognate phosphatase Stp dephosphorylates these phosphorylation sites. Moreover, Stk interacts with FemA and FemB, but is unable to phosphorylate them. Our data indicate that Stk and Stp modulate cell wall synthesis and cell division at several levels.},
  language  = {en}
}
@article{WanZhangPruittetal.2019,
  author    = {Wan, Wei-Lin and Zhang, Lisha and Pruitt, Rory and Zaidem, Maricris and Brugman, Rik and Ma, Xiyu and Krol, Elzbieta and Perraki, Artemis and Kilian, Joachim and Grossmann, Guido and Stahl, Mark and Shan, Libo and Zipfel, Cyril and van Kan, Jan A. L. and Hedrich, Rainer and Weigel, Detlef and Gust, Andrea A. and N{\"u}rnberger, Thorsten},
  title     = {Comparing Arabidopsis receptor kinase and receptor protein-mediated immune signaling reveals BIK1-dependent differences},
  series = {New Phytologist},
  volume    = {221},
  journal   = {New Phytologist},
  doi       = {10.1111/nph.15497},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-233385},
  pages     = {2080-2095},
  year      = {2019},
  abstract  = {Pattern recognition receptors (PRRs) sense microbial patterns and activate innate immunity against attempted microbial invasions. The leucine-rich repeat receptor kinases (LRR-RK) FLS2 and EFR, and the LRR receptor protein (LRR-RP) receptors RLP23 and RLP42, respectively, represent prototypical members of these two prominent and closely related PRR families. We conducted a survey of Arabidopsis thaliana immune signaling mediated by these receptors to address the question of commonalities and differences between LRR-RK and LRR-RP signaling. Quantitative differences in timing and amplitude were observed for several early immune responses, with RP-mediated responses typically being slower and more prolonged than those mediated by RKs. Activation of RLP23, but not FLS2, induced the production of camalexin. Transcriptomic analysis revealed that RLP23-regulated genes represent only a fraction of those genes differentially expressed upon FLS2 activation. Several positive and negative regulators of FLS2-signaling play similar roles in RLP23 signaling. Intriguingly, the cytoplasmic receptor kinase BIK1, a positive regulator of RK signaling, acts as a negative regulator of RP-type immune receptors in a manner dependent on BIK1 kinase activity. Our study unveiled unexpected differences in two closely related receptor systems and reports a new negative role of BIK1 in plant immunity.},
  language  = {en}
}