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@ARTICLE{Lzaro:282474,
      author       = {Lázaro, Diana F and Amen, Triana and Gerhardt, Ellen and
                      Song, Chengyuan and Burns, Ryan and Kruse, Niels and Santos,
                      Patrícia I and Milovanovic, Dragomir and Höglinger,
                      Günter and Mollenhauer, Brit and Luk, Kelvin C and Lee,
                      Virginia My- and Outeiro, Tiago F},
      title        = {{S}ynphilin-1 modulates alpha-synuclein assembly, release
                      and uptake.},
      journal      = {npj Parkinson's Disease},
      volume       = {11},
      number       = {1},
      issn         = {2373-8057},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2025-01297},
      pages        = {326},
      year         = {2025},
      abstract     = {Alpha-synuclein (aSyn) is an intrinsically disordered
                      protein involved in phase separation and several
                      age-associated neurodegenerative disorders, including
                      Parkinson's disease. However, its function and pathological
                      role remain elusive. Here, we modeled different aSyn
                      assemblies in living cells by exploiting its interaction
                      with synphilin-1 (Sph1). We developed a model that reports
                      on gel- and solid-like inclusions through coexpression of
                      aSyn and Sph1. Distinct morphological differences emerged
                      between VN-aSyn + aSyn-VC and VN-Sph1 + aSyn-VC assemblies,
                      showing unique antibody recognition, proteinase K
                      resistance, and protein mobilities. The VN-Sph1 + aSyn-VC
                      interaction could be manipulated to alter inclusion size and
                      number. These inclusions also contained lysosomes and AP-1
                      vesicles, aligning with observations in human brain tissue.
                      Our study offers new insight into aSyn aggregation and
                      release, highlighting the importance of Sph1 and other
                      aSyn-interacting proteins in synucleinopathies, which
                      involve diverse copathologies only now beginning to be
                      understood.},
      cin          = {AG Fischer / AG Milovanovic (Berlin) / Clinical Research
                      (Munich)},
      ddc          = {610},
      cid          = {I:(DE-2719)1410002 / I:(DE-2719)1813002 /
                      I:(DE-2719)1111015},
      pnm          = {352 - Disease Mechanisms (POF4-352) / 351 - Brain Function
                      (POF4-351) / 353 - Clinical and Health Care Research
                      (POF4-353)},
      pid          = {G:(DE-HGF)POF4-352 / G:(DE-HGF)POF4-351 /
                      G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41266386},
      doi          = {10.1038/s41531-025-01144-3},
      url          = {https://pub.dzne.de/record/282474},
}