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@ARTICLE{RugerHerreros:287680,
      author       = {C. Ruger-Herreros and L. Svoboda and A. Mogk and B.
                      Bukau$^*$},
      title        = {{R}ole of {J}-domain proteins in yeast physiology and
                      protein quality control.},
      journal      = {Journal of molecular biology},
      volume       = {436},
      number       = {14},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2024-00308},
      pages        = {168484},
      year         = {2024},
      note         = {DKFZ-ZMBH Alliance / #LA:A250# / 2024 Jul
                      15;436(14):168484},
      abstract     = {The Hsp70 chaperone system is a central component of
                      cellular protein quality control (PQC) by acting in a
                      multitude of protein folding processes ranging from the
                      folding of newly synthesized proteins to the disassembly and
                      refolding of protein aggregates. This multifunctionality of
                      Hsp70 is governed by J-domain proteins (JDPs), which act as
                      indispensable co-chaperones that target specific substrates
                      to Hsp70. The numbers of distinct JDPs present in a species
                      always outnumbers Hsp70, documenting JDP function in
                      functional diversification of Hsp70. In this review, we
                      describe the physiological roles of JDPs in the
                      Saccharomyces cerevisiae PQC system, with a focus on the
                      abundant JDP generalists, Zuo1, Ydj1 and Sis1, which
                      function in fundamental cellular processes. Ribosome-bound
                      Zuo1 cooperates with the Hsp70 chaperones Ssb1/2 in folding
                      and assembly of nascent polypeptides. Ydj1 and Sis1
                      cooperate with the Hsp70 members Ssa1 to Ssa4 to exert
                      overlapping functions in protein folding and targeting of
                      newly synthesized proteins to organelles including
                      mitochondria and facilitating the degradation of aberrant
                      proteins by E3 ligases. Furthermore, they act in protein
                      disaggregation reactions, though Ydj1 and Sis1 differ in
                      their modes of Hsp70 cooperation and substrate
                      specificities. This results in functional specialization as
                      seen in prion propagation and the underlying dominant role
                      of Sis1 in targeting Hsp70 for shearing of prion amyloid
                      fibrils.},
      subtyp        = {Review Article},
      cin          = {A250},
      ddc          = {610},
      cid          = {I:(DE-He78)A250-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38331212},
      doi          = {10.1016/j.jmb.2024.168484},
      url          = {https://inrepo02.dkfz.de/record/287680},
}