% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Zaffagnini:856514,
      author       = {Zaffagnini, G. and Savova, A. and Danieli, A. and Romanov,
                      J. and Tremel, S. and Ebner, M. and Peterbauer, T. and
                      Sztacho, M. and Trapannone, R. and Tarafder, A. K. and
                      Sachse, Carsten and Martens, S.},
      title        = {{P}hasing out the bad-{H}ow {SQSTM}1/p62 sequesters
                      ubiquitinated proteins for degradation by autophagy},
      journal      = {Autophagy},
      volume       = {14},
      number       = {7},
      issn         = {1554-8627},
      address      = {Abingdon, Oxon},
      publisher    = {Taylor $\&$ Francis},
      reportid     = {FZJ-2018-05901},
      pages        = {1280-1282},
      year         = {2018},
      abstract     = {The degradation of misfolded, ubiquitinated proteins is
                      essential for cellular homeostasis. These proteins are
                      primarily degraded by the ubiquitin-proteasome system (UPS)
                      and macroautophagy/autophagy serves as a backup mechanism
                      when the UPS is overloaded. How autophagy and the UPS are
                      coordinated is not fully understood. During the autophagy of
                      misfolded, ubiquitinated proteins, referred to as
                      aggrephagy, substrate proteins are clustered into larger
                      structures in a SQSTM1/p62-dependent manner before they are
                      sequestered by phagophores, the precursors to
                      autophagosomes. We have recently shown that SQSTM1/p62 and
                      ubiquitinated proteins spontaneously phase separate into
                      micrometer-sized clusters in vitro. This enabled us to
                      characterize the properties of the ubiquitin-positive
                      substrates that are necessary for the SQSTM1/p62-mediated
                      cluster formation. Our results suggest that aggrephagy is
                      triggered by the accumulation of substrates with multiple
                      ubiquitin chains and that the process can be inhibited by
                      active proteasomes.},
      cin          = {ER-C-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29929426},
      UT           = {WOS:000441624100020},
      doi          = {10.1080/15548627.2018.1462079},
      url          = {https://juser.fz-juelich.de/record/856514},
}