@article{JaślanDreyerLuetal.2019,
  author    = {Jaślan, Dawid and Dreyer, Ingo and Lu, Jinping and O'Malley, Ronan and Dindas, Julian and Marten, Irene and Hedrich, Rainer},
  title     = {Voltage-dependent gating of SV channel TPC1 confers vacuole excitability},
  series = {Nature Communications},
  volume    = {10},
  journal   = {Nature Communications},
  doi       = {10.1038/s41467-019-10599-x},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-202029},
  pages     = {2659},
  year      = {2019},
  abstract  = {In contrast to the plasma membrane, the vacuole membrane has not yet been associated with electrical excitation of plants. Here, we show that mesophyll vacuoles from Arabidopsis sense and control the membrane potential essentially via the K\(^+\)-permeable TPC1 and TPK channels. Electrical stimuli elicit transient depolarization of the vacuole membrane that can last for seconds. Electrical excitability is suppressed by increased vacuolar Ca\(^{2+}\) levels. In comparison to wild type, vacuoles from the fou2 mutant, harboring TPC1 channels insensitive to luminal Ca\(^{2+}\), can be excited fully by even weak electrical stimuli. The TPC1-loss-of-function mutant tpc1-2 does not respond to electrical stimulation at all, and the loss of TPK1/TPK3-mediated K\(^{+}\) transport affects the duration of TPC1-dependent membrane depolarization. In combination with mathematical modeling, these results show that the vacuolar K\(^+\)-conducting TPC1 and TPK1/TPK3 channels act in concert to provide for Ca\(^{2+}\)- and voltage-induced electrical excitability to the central organelle of plant cells.},
  language  = {en}
}
@article{LiuMaierhoferRybaketal.2019,
  author    = {Liu, Yi and Maierhofer, Tobias and Rybak, Katarzyna and Sklenar, Jan and Breakspear, Andy and Johnston, Matthew G. and Fliegmann, Judith and Huang, Shouguang and Roelfsema, M. Rob G. and Felix, Georg and Faulkner, Christine and Menke, Frank L.H. and Geiger, Dietmar and Hedrich, Rainer and Robatzek, Silke},
  title     = {Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure},
  series = {eLife},
  volume    = {8},
  journal   = {eLife},
  doi       = {10.7554/eLife.44474},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-202631},
  pages     = {e44474},
  year      = {2019},
  abstract  = {In plants, antimicrobial immune responses involve the cellular release of anions and are responsible for the closure of stomatal pores. Detection of microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) induces currents mediated via slow-type (S-type) anion channels by a yet not understood mechanism. Here, we show that stomatal closure to fungal chitin is conferred by the major PRRs for chitin recognition, LYK5 and CERK1, the receptor-like cytoplasmic kinase PBL27, and the SLAH3 anion channel. PBL27 has the capacity to phosphorylate SLAH3, of which S127 and S189 are required to activate SLAH3. Full activation of the channel entails CERK1, depending on PBL27. Importantly, both S127 and S189 residues of SLAH3 are required for chitin-induced stomatal closure and anti-fungal immunity at the whole leaf level. Our results demonstrate a short signal transduction module from MAMP recognition to anion channel activation, and independent of ABA-induced SLAH3 activation.},
  language  = {en}
}