@article{NguyenSchippersGoniRamosetal.2013,
  author    = {Nguyen, Hung M. and Schippers, Jos H. M. and Goni-Ramos, Oscar and Christoph, Mathias P. and Dortay, Hakan and van der Hoorn, Renier A. L. and M{\"u}ller-R{\"o}ber, Bernd},
  title     = {An upstream regulator of the 26S proteasome modulates organ size in Arabidopsis thaliana},
  series = {The plant journal},
  volume    = {74},
  journal   = {The plant journal},
  number    = {1},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {0960-7412},
  doi       = {10.1111/tpj.12097},
  pages     = {25 -- 36},
  year      = {2013},
  abstract  = {In both animal and plant kingdoms, body size is a fundamental but still poorly understood attribute of biological systems. Here we report that the Arabidopsis NAC transcription factor Regulator of Proteasomal Gene Expression' (RPX) controls leaf size by positively modulating proteasome activity. We further show that the cis-element recognized by RPX is evolutionarily conserved between higher plant species. Upon over-expression of RPX, plants exhibit reduced growth, which may be reversed by a low concentration of the pharmacological proteasome inhibitor MG132. These data suggest that the rate of protein turnover during growth is a critical parameter for determining final organ size.},
  language  = {en}
}
@misc{UestuenBoernke2014,
  author    = {Uestuen, Suayib and B{\"o}rnke, Frederik},
  title     = {Interactions of Xanthomonas type-III effector proteins with the plant ubiquitin and ubiquitin-like pathways},
  series = {Frontiers in plant science},
  volume    = {5},
  journal   = {Frontiers in plant science},
  publisher = {Frontiers Research Foundation},
  address   = {Lausanne},
  issn      = {1664-462X},
  doi       = {10.3389/fpls.2014.00736},
  pages     = {6},
  year      = {2014},
  abstract  = {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.},
  language  = {en}
}
@article{WendlerEnenkel2019,
  author    = {Wendler, Petra and Enenkel, Cordula},
  title     = {Nuclear Transport of Yeast Proteasomes},
  series = {Frontiers in molecular biosciences},
  volume    = {6},
  journal   = {Frontiers in molecular biosciences},
  publisher = {Frontiers Research Foundation},
  address   = {Lausanne},
  issn      = {2296-889X},
  doi       = {10.3389/fmolb.2019.00034},
  pages     = {12},
  year      = {2019},
  abstract  = {Proteasomes are key proteases in regulating protein homeostasis. Their holo-enzymes are composed of 40 different subunits which are arranged in a proteolytic core (CP) flanked by one to two regulatory particles (RP). Proteasomal proteolysis is essential for the degradation of proteins which control time-sensitive processes like cell cycle progression and stress response. In dividing yeast and human cells, proteasomes are primarily nuclear suggesting that proteasomal proteolysis is mainly required in the nucleus during cell proliferation. In yeast, which have a closed mitosis, proteasomes are imported into the nucleus as immature precursors via the classical import pathway. During quiescence, the reversible absence of proliferation induced by nutrient depletion or growth factor deprivation, proteasomes move from the nucleus into the cytoplasm. In the cytoplasm of quiescent yeast, proteasomes are dissociated into CP and RP and stored in membrane-less cytoplasmic foci, named proteasome storage granules (PSGs). With the resumption of growth, PSGs clear and mature proteasomes are transported into the nucleus by Blm10, a conserved 240 kDa protein and proteasome-intrinsic import receptor. How proteasomes are exported from the nucleus into the cytoplasm is unknown.},
  language  = {en}
}