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@ARTICLE{Ho:147392,
      author       = {C.-T. Ho$^*$ and T. Grousl$^*$ and O. Shatz$^*$ and A.
                      Jawed$^*$ and C. Ruger-Herreros$^*$ and M. Semmelink$^*$ and
                      R. Zahn$^*$ and K. Richter$^*$ and B. Bukau$^*$ and A.
                      Mogk$^*$},
      title        = {{C}ellular sequestrases maintain basal {H}sp70 capacity
                      ensuring balanced proteostasis.},
      journal      = {Nature Communications},
      volume       = {10},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DKFZ-2019-02509},
      pages        = {4851},
      year         = {2019},
      note         = {DKFZ-ZMBH Alliance},
      abstract     = {Maintenance of cellular proteostasis is achieved by a
                      multi-layered quality control network, which counteracts the
                      accumulation of misfolded proteins by refolding and
                      degradation pathways. The organized sequestration of
                      misfolded proteins, actively promoted by cellular
                      sequestrases, represents a third strategy of quality
                      control. Here we determine the role of sequestration within
                      the proteostasis network in Saccharomyces cerevisiae and the
                      mechanism by which it occurs. The Hsp42 and Btn2
                      sequestrases are functionally intertwined with the refolding
                      activity of the Hsp70 system. Sequestration of misfolded
                      proteins by Hsp42 and Btn2 prevents proteostasis collapse
                      and viability loss in cells with limited Hsp70 capacity,
                      likely by shielding Hsp70 from misfolded protein overload.
                      Btn2 has chaperone and sequestrase activity and shares
                      features with small heat shock proteins. During stress
                      recovery Btn2 recruits the Hsp70-Hsp104 disaggregase by
                      directly interacting with the Hsp70 co-chaperone Sis1,
                      thereby shunting sequestered proteins to the refolding
                      pathway.},
      cin          = {A250 / W230},
      ddc          = {500},
      cid          = {I:(DE-He78)A250-20160331 / I:(DE-He78)W230-20160331},
      pnm          = {321 - Basic Concepts (POF3-321)},
      pid          = {G:(DE-HGF)POF3-321},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31649258},
      pmc          = {pmc:PMC6813348},
      doi          = {10.1038/s41467-019-12868-1},
      url          = {https://inrepo02.dkfz.de/record/147392},
}