@article{LiuVainViottietal.2018,
  author    = {Liu, Qinsong and Vain, Thomas and Viotti, Corrado and Doyle, Siamsa M. and Tarkowska, Danuse and Novak, Ondrej and Zipfel, Cyril and Sitbon, Folke and Robert, Stephanie and Hofius, Daniel},
  title     = {Vacuole integrity maintained by DUF300 proteins is required for brassinosteroid signaling regulation},
  series = {Molecular plant},
  volume    = {11},
  journal   = {Molecular plant},
  number    = {4},
  publisher = {Cell Press},
  address   = {Cambridge},
  issn      = {1674-2052},
  doi       = {10.1016/j.molp.2017.12.015},
  pages     = {553 -- 567},
  year      = {2018},
  abstract  = {Brassinosteroid (BR) hormone signaling controls multiple processes during plant growth and development and is initiated at the plasma membrane through the receptor kinase BRASSINOSTEROID INSENSITIVE1 (BRI1) together with co-receptors such as BRI1-ASSOCIATED RECEPTOR KINASE1 (BAK1). BRI1 abundance is regulated by endosomal recycling and vacuolar targeting, but the role of vacuole-related proteins in BR receptor dynamics and BR responses remains elusive. Here, we show that the absence of two DUF300 domain-containing tonoplast proteins, LAZARUS1 (LAZ1) and LAZ1 HOMOLOG1 (LAZ1H1), causes vacuole morphology defects, growth inhibition, and constitutive activation of BR signaling. Intriguingly, tonoplast accumulation of BAK1 was substantially increased and appeared causally linked to enhanced BRI1 trafficking and degradation in laz1 laz1h1 plants. Since unrelated vacuole mutants exhibited normal BR responses, our findings indicate that DUF300 proteins play distinct roles in the regulation of BR signaling by maintaining vacuole integrity required to balance subcellular BAK1 pools and BR receptor distribution.},
  language  = {en}
}
@article{LeongRaffeinerSpintietal.2022,
  author    = {Leong, Jia Xuan and Raffeiner, Margot and Spinti, Daniela and Langin, Gautier and Franz-Wachtel, Mirita and Guzman, Andrew R. and Kim, Jung-Gun and Pandey, Pooja and Minina, Alyona E. and Macek, Boris and Hafren, Anders and Bozkurt, Tolga O. and Mudgett, Mary Beth and B{\"o}rnke, Frederik and Hofius, Daniel and Uestuen, Suayib},
  title     = {A bacterial effector counteracts host autophagy by promoting degradation of an autophagy component},
  series = {The EMBO journal},
  volume    = {41},
  journal   = {The EMBO journal},
  number    = {13},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {0261-4189},
  doi       = {10.15252/embj.2021110352},
  pages     = {17},
  year      = {2022},
  abstract  = {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.},
  language  = {en}
}