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100 1 _ |a Lázaro, Diana F
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245 _ _ |a Synphilin-1 modulates alpha-synuclein assembly, release and uptake.
260 _ _ |a [London]
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520 _ _ |a 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.
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700 1 _ |a Amen, Triana
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700 1 _ |a Gerhardt, Ellen
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700 1 _ |a Song, Chengyuan
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700 1 _ |a Burns, Ryan
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700 1 _ |a Luk, Kelvin C
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773 _ _ |a 10.1038/s41531-025-01144-3
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