% 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{Hoffmann:154773,
      author       = {Hoffmann, Christian and Sansevrino, Roberto and Morabito,
                      Giuseppe and Logan, Chinyere and Vabulas, R Martin and
                      Ulusoy, Ayse and Ganzella, Marcelo and Milovanovic,
                      Dragomir},
      title        = {{S}ynapsin {C}ondensates {R}ecruit alpha-{S}ynuclein.},
      journal      = {Journal of molecular biology},
      volume       = {433},
      number       = {12},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2021-00363},
      pages        = {166961},
      year         = {2021},
      abstract     = {Neurotransmission relies on the tight spatial and temporal
                      regulation of the synaptic vesicle (SV) cycle. Nerve
                      terminals contain hundreds of SVs that form tight clusters.
                      These clusters represent a distinct liquid phase in which
                      one component of the phase are SVs and the other synapsin 1,
                      a highly abundant synaptic protein. Another major family of
                      disordered proteins at the presynapse includes synucleins,
                      most notably α-synuclein. The precise physiological role of
                      α-synuclein in synaptic physiology remains elusive, albeit
                      its role has been implicated in nearly all steps of the SV
                      cycle. To determine the effect of α-synuclein on the
                      synapsin phase, we employ the reconstitution approach using
                      natively purified SVs from rat brains and the heterologous
                      cell system to generate synapsin condensates. We demonstrate
                      that synapsin condensates recruit α-synuclein, and while
                      enriched into these synapsin condensates, α-synuclein still
                      maintains its high mobility. The presence of SVs enhances
                      the rate of synapsin/α-synuclein condensation, suggesting
                      that SVs act as catalyzers for the formation of synapsin
                      condensates. Notably, at physiological salt and protein
                      concentrations, α-synuclein alone is not able to cluster
                      isolated SVs. Excess of α-synuclein disrupts the kinetics
                      of synapsin/SV condensate formation, indicating that the
                      molar ratio between synapsin and α-synuclein is important
                      in assembling the functional condensates of SVs.
                      Understanding the molecular mechanism of α-synuclein
                      interactions at the nerve terminals is crucial for
                      clarifying the pathogenesis of synucleinopathies, where
                      α-synuclein, synaptic proteins and lipid organelles all
                      accumulate as insoluble intracellular inclusions.},
      keywords     = {Animals / Brain: cytology / Brain: metabolism / HEK293
                      Cells / Humans / Luminescent Proteins: genetics /
                      Luminescent Proteins: metabolism / Macromolecular
                      Substances: chemistry / Macromolecular Substances:
                      metabolism / Microscopy, Confocal / Microscopy, Fluorescence
                      / Rats / Synapsins: chemistry / Synapsins: metabolism /
                      Synaptic Transmission / Synaptic Vesicles: metabolism /
                      alpha-Synuclein: chemistry / alpha-Synuclein: metabolism /
                      liquid-liquid phase separation (Other) / synapsin 1 (Other)
                      / synaptic vesicles (Other) / synucleinopathies (Other) /
                      α-synuclein (Other)},
      cin          = {AG Milovanovic ; AG Milovanovic / AG Di Monte},
      ddc          = {610},
      cid          = {I:(DE-2719)1813002 / I:(DE-2719)1013008},
      pnm          = {351 - Brain Function (POF4-351) / 352 - Disease Mechanisms
                      (POF4-352)},
      pid          = {G:(DE-HGF)POF4-351 / G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33774037},
      doi          = {10.1016/j.jmb.2021.166961},
      url          = {https://pub.dzne.de/record/154773},
}