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@INBOOK{Hochmair:165615,
      author       = {Hochmair, Janine and Exner, Christian and Betzel, Christian
                      and Mandelkow, Eckhard and Wegmann, Susanne},
      title        = {{L}ight {M}icroscopy and {D}ynamic {L}ight {S}cattering to
                      {S}tudy {L}iquid-{L}iquid {P}hase {S}eparation of {T}au
                      {P}roteins {I}n {V}itro.},
      volume       = {2551},
      address      = {New York, NY},
      publisher    = {Springer US},
      reportid     = {DZNE-2022-01748},
      isbn         = {978-1-0716-2596-5 (print)},
      series       = {Methods in Molecular Biology},
      pages        = {225 - 243},
      year         = {2023},
      comment      = {Protein Aggregation / Cieplak, Andrzej Stanisław (Editor)
                      ; New York, NY : Springer US, 2023, Chapter 15 ; ISSN:
                      1064-3745=1940-6029 ; ISBN:
                      978-1-0716-2596-5=978-1-0716-2597-2 ;
                      doi:10.1007/978-1-0716-2597-2},
      booktitle     = {Protein Aggregation / Cieplak, Andrzej
                       Stanisław (Editor) ; New York, NY :
                       Springer US, 2023, Chapter 15 ; ISSN:
                       1064-3745=1940-6029 ; ISBN:
                       978-1-0716-2596-5=978-1-0716-2597-2 ;
                       doi:10.1007/978-1-0716-2597-2},
      abstract     = {Tau is an intrinsically disordered protein that binds and
                      stabilizes axonal microtubules (MTs) in neurons of the
                      central nervous system. The binding of Tau to MTs is
                      mediated by its repeat domain and flanking proline-rich
                      domains. The positively charged (basic) C-terminal half of
                      Tau also mediates the assembly Tau into fibrillar aggregates
                      in Alzheimer's disease (AD) and tauopathy brains. In recent
                      years, another assembly form of Tau has been identified: Tau
                      can undergo liquid-liquid phase separation (LLPS), which
                      leads to its condensation into liquid-dense phases, either
                      by complex coacervation with polyanions like heparin or RNA
                      or through 'self-coacervation' at high Tau concentrations.
                      Condensation of Tau in the absence of polyanions can be
                      enhanced by the presence of molecular crowding agents in a
                      dilute Tau solution. In vitro experiments using recombinant
                      purified Tau are helpful to study the physicochemical
                      determinants of Tau LLPS, which can then be extrapolated
                      into the cellular context. Tau condensation is a new aspect
                      of Tau biology that may play a role for the initiation of
                      Tau aggregation, but also for its physiological function(s),
                      for example, the binding to microtubules. Here we describe
                      how to study the condensation of Tau in vitro using light
                      microscopy, including fluorescence recovery after
                      photobleaching (FRAP), to assess the shape and molecular
                      diffusion in the condensates, a proxy for the degree of
                      condensate percolation. We also describe turbidity
                      measurements of condensate-containing solutions to assess
                      the overall amount of LLPS and time-resolved dynamic light
                      scattering (trDLS) to study the formation and size of Tau
                      condensates.},
      keywords     = {Humans / tau Proteins: metabolism / Microscopy / Dynamic
                      Light Scattering / Alzheimer Disease: metabolism /
                      Coacervation (Other) / Condensation (Other) / Crowding
                      agents (Other) / FRAP (Other) / LLPS (Other) / MAPT (Other)
                      / Polyethylene glycol (Other) / RNA (Other) / tau Proteins
                      (NLM Chemicals) / polyanions (NLM Chemicals)},
      cin          = {AG Wegmann / AG Mandelkow 1},
      ddc          = {570},
      cid          = {I:(DE-2719)1810006 / I:(DE-2719)1013014},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)7},
      pubmed       = {pmid:36310206},
      doi          = {10.1007/978-1-0716-2597-2_15},
      url          = {https://pub.dzne.de/record/165615},
}