@article{KoernerMeyerMarincolaetal.2023,
  author    = {K{\"o}rner, Maria and Meyer, Susanne R. and Marincola, Gabriella and Kern, Maximilian J. and Grimm, Clemens and Schuelein-Voelk, Christina and Fischer, Utz and Hofmann, Kay and Buchberger, Alexander},
  title     = {The FAM104 proteins VCF1/2 promote the nuclear localization of p97/VCP},
  series = {eLife},
  volume    = {12},
  journal   = {eLife},
  doi       = {10.7554/eLife.92409},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-350222},
  year      = {2023},
  abstract  = {The ATPase p97 (also known as VCP, Cdc48) has crucial functions in a variety of important cellular processes such as protein quality control, organellar homeostasis, and DNA damage repair, and its de-regulation is linked to neuromuscular diseases and cancer. p97 is tightly controlled by numerous regulatory cofactors, but the full range and function of the p97-cofactor network is unknown. Here, we identify the hitherto uncharacterized FAM104 proteins as a conserved family of p97 interactors. The two human family members VCP nuclear cofactor family member 1 and 2 (VCF1/2) bind p97 directly via a novel, alpha-helical motif and associate with p97-UFD1-NPL4 and p97-UBXN2B complexes in cells. VCF1/2 localize to the nucleus and promote the nuclear import of p97. Loss of VCF1/2 results in reduced nuclear p97 levels, slow growth, and hypersensitivity to chemical inhibition of p97 in the absence and presence of DNA damage, suggesting that FAM104 proteins are critical regulators of nuclear p97 functions.},
  language  = {en}
}
@article{PascoalinoDindarVieiradaRochaetal.2014,
  author    = {Pascoalino, Bruno and Dindar, G{\"u}lcin and Vieira-da-Rocha, Jo{\~a}o P. and Machado, Carlos Renato and Janzen, Christian J. and Schenkman, Sergio},
  title     = {Characterization of two different Asf1 histone chaperones with distinct cellular localizations and functions in Trypanosoma brucei},
  series = {Nucleic Acids Research},
  volume    = {42},
  journal   = {Nucleic Acids Research},
  number    = {5},
  issn      = {1362-4962},
  doi       = {10.1093/nar/gkt1267},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-117220},
  pages     = {2906-2918},
  year      = {2014},
  abstract  = {The anti-silencing function protein 1 (Asf1) is a chaperone that forms a complex with histones H3 and H4 facilitating dimer deposition and removal from chromatin. Most eukaryotes possess two different Asf1 chaperones but their specific functions are still unknown. Trypanosomes, a group of early-diverged eukaryotes, also have two, but more divergent Asf1 paralogs than Asf1 of higher eukaryotes. To unravel possible different functions, we characterized the two Asf1 proteins in Trypanosoma brucei. Asf1A is mainly localized in the cytosol but translocates to the nucleus in S phase. In contrast, Asf1B is predominantly localized in the nucleus, as described for other organisms. Cytosolic Asf1 knockdown results in accumulation of cells in early S phase of the cell cycle, whereas nuclear Asf1 knockdown arrests cells in S/G2 phase. Overexpression of cytosolic Asf1 increases the levels of histone H3 and H4 acetylation. In contrast to cytosolic Asf1, overexpression of nuclear Asf1 causes less pronounced growth defects in parasites exposed to genotoxic agents, prompting a function in chromatin remodeling in response to DNA damage. Only the cytosolic Asf1 interacts with recombinant H3/H4 dimers in vitro. These findings denote the early appearance in evolution of distinguishable functions for the two Asf1 chaperons in trypanosomes.},
  language  = {en}
}