@article{KuckelkornStueblerTextorisTaubeetal.2019,
  author    = {Kuckelkorn, Ulrike and St{\"u}bler, Sabine and Textoris-Taube, Kathrin and Kilian, Christiane and Niewienda, Agathe and Henklein, Petra and Janek, Katharina and Stumpf, Michael P. H. and Mishto, Michele and Liepe, Juliane},
  title     = {Proteolytic dynamics of human 20S thymoproteasome},
  series = {The journal of biological chemistry},
  volume    = {294},
  journal   = {The journal of biological chemistry},
  number    = {19},
  publisher = {American Society for Biochemistry and Molecular Biology},
  address   = {Bethesda},
  issn      = {1083-351X},
  doi       = {10.1074/jbc.RA118.007347},
  pages     = {7740 -- 7754},
  year      = {2019},
  abstract  = {An efficient immunosurveillance of CD8(+) T cells in the periphery depends on positive/negative selection of thymocytes and thus on the dynamics of antigen degradation and epitope production by thymoproteasome and immunoproteasome in the thymus. Although studies in mouse systems have shown how thymoproteasome activity differs from that of immunoproteasome and strongly impacts the T cell repertoire, the proteolytic dynamics and the regulation of human thymoproteasome are unknown. By combining biochemical and computational modeling approaches, we show here that human 20S thymoproteasome and immunoproteasome differ not only in the proteolytic activity of the catalytic sites but also in the peptide transport. These differences impinge upon the quantity of peptide products rather than where the substrates are cleaved. The comparison of the two human 20S proteasome isoforms depicts different processing of antigens that are associated to tumors and autoimmune diseases.},
  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}
}