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@ARTICLE{Jackson:269354,
      author       = {Jackson, Joshua and Hoffmann, Christian and Scifo, Enzo and
                      Wang, Han and Wischhof, Lena and Piazzesi, Antonia and
                      Mondal, Mrityunjoy and Shields, Hanna and Zhou, Xuesi and
                      Mondin, Magali and Ryan, Eanna B and Döring, Hermann and
                      Prehn, Jochen H M and Rottner, Klemens and Giannone, Gregory
                      and Nicotera, Pierluigi and Ehninger, Dan and Milovanovic,
                      Dragomir and Bano, Daniele},
      title        = {{A}ctin-nucleation promoting factor {N}-{WASP} influences
                      alpha-synuclein condensates and pathology.},
      journal      = {Cell death $\&$ disease},
      volume       = {15},
      number       = {4},
      issn         = {2041-4889},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {DZNE-2024-00522},
      pages        = {304},
      year         = {2024},
      abstract     = {Abnormal intraneuronal accumulation of soluble and
                      insoluble α-synuclein (α-Syn) is one of the main
                      pathological hallmarks of synucleinopathies, such as
                      Parkinson's disease (PD). It has been well documented that
                      the reversible liquid-liquid phase separation of α-Syn can
                      modulate synaptic vesicle condensates at the presynaptic
                      terminals. However, α-Syn can also form liquid-like
                      droplets that may convert into amyloid-enriched hydrogels or
                      fibrillar polymorphs under stressful conditions. To advance
                      our understanding on the mechanisms underlying α-Syn phase
                      transition, we employed a series of unbiased proteomic
                      analyses and found that actin and actin regulators are part
                      of the α-Syn interactome. We focused on Neural
                      Wiskott-Aldrich syndrome protein (N-WASP) because of its
                      association with a rare early-onset familial form of PD. In
                      cultured cells, we demonstrate that N-WASP undergoes phase
                      separation and can be recruited to synapsin 1 liquid-like
                      droplets, whereas it is excluded from α-Syn/synapsin 1
                      condensates. Consistently, we provide evidence that
                      wsp-1/WASL loss of function alters the number and dynamics
                      of α-Syn inclusions in the nematode Caenorhabditis elegans.
                      Together, our findings indicate that N-WASP expression may
                      create permissive conditions that promote α-Syn condensates
                      and their potentially deleterious conversion into toxic
                      species.},
      keywords     = {alpha-Synuclein: metabolism / Animals / Humans /
                      Caenorhabditis elegans: metabolism / Wiskott-Aldrich
                      Syndrome Protein, Neuronal: metabolism / Actins: metabolism
                      / Parkinson Disease: metabolism / Parkinson Disease:
                      pathology / Synapsins: metabolism / Caenorhabditis elegans
                      Proteins: metabolism / alpha-Synuclein (NLM Chemicals) /
                      Wiskott-Aldrich Syndrome Protein, Neuronal (NLM Chemicals) /
                      Actins (NLM Chemicals) / WASL protein, human (NLM Chemicals)
                      / Synapsins (NLM Chemicals) / Caenorhabditis elegans
                      Proteins (NLM Chemicals)},
      cin          = {AG Bano / AG Milovanovic / AG Ehninger},
      ddc          = {570},
      cid          = {I:(DE-2719)1013003 / I:(DE-2719)1813002 /
                      I:(DE-2719)1013005},
      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},
      pmc          = {pmc:PMC11063037},
      pubmed       = {pmid:38693139},
      doi          = {10.1038/s41419-024-06686-7},
      url          = {https://pub.dzne.de/record/269354},
}