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@ARTICLE{Reinle:169862,
      author       = {K. Reinle and A. Mogk and B. Bukau$^*$},
      title        = {{T}he diverse functions of small heat shock proteins in the
                      proteostasis network.},
      journal      = {Journal of molecular biology},
      volume       = {434},
      number       = {1},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2021-01596},
      pages        = {167157},
      year         = {2022},
      note         = {#LA:A250# /2022 Jan 15;434(1):167157 / DKFZ-ZMBH Alliance},
      abstract     = {The protein quality control (PQC) system maintains protein
                      homeostasis by counteracting the accumulation of misfolded
                      protein conformers. Substrate degradation and refolding
                      activities executed by ATP-dependent proteases and
                      chaperones constitute major strategies of the proteostasis
                      network. Small heat shock proteins represent ATP-independent
                      chaperones that bind to misfolded proteins, preventing their
                      uncontrolled aggregation. sHsps share the conserved
                      α-crystallin domain (ACD) and gain functional specificity
                      through variable and largely disordered N- and C-terminal
                      extensions (NTE, CTE). They form large, polydisperse
                      oligomers through multiple, weak interactions between
                      NTE/CTEs and ACD dimers. Sequence variations of sHsps and
                      the large variability of sHsp oligomers enable sHsps to
                      fulfill diverse tasks in the PQC network. sHsp oligomers
                      represent inactive yet dynamic resting states that are
                      rapidly deoligomerized and activated upon stress conditions,
                      releasing substrate binding sites in NTEs and ACDs Bound
                      substrates are usually isolated in large sHsp/substrate
                      complexes. This sequestration activity of sHsps represents a
                      third strategy of the proteostasis network. Substrate
                      sequestration reduces the burden for other PQC components
                      during immediate and persistent stress conditions.
                      Sequestered substrates can be released and directed towards
                      refolding pathways by ATP-dependent Hsp70/Hsp100 chaperones
                      or sorted for degradation by autophagic pathways. sHsps can
                      also maintain the dynamic state of phase-separated stress
                      granules (SGs), which store mRNA and translation factors, by
                      reducing the accumulation of misfolded proteins inside SGs
                      and preventing unfolding of SG components. This ensures SG
                      disassembly and regain of translational capacity during
                      recovery periods.},
      subtyp        = {Review Article},
      keywords     = {chaperone (Other) / protein aggregation (Other) /
                      proteostasis (Other) / small heat shock protein (Other) /
                      stress granule (Other)},
      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:34271010},
      doi          = {10.1016/j.jmb.2021.167157},
      url          = {https://inrepo02.dkfz.de/record/169862},
}