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000282474 1001_ $$aLázaro, Diana F$$b0
000282474 245__ $$aSynphilin-1 modulates alpha-synuclein assembly, release and uptake.
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000282474 520__ $$aAlpha-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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000282474 7001_ $$aAmen, Triana$$b1
000282474 7001_ $$aGerhardt, Ellen$$b2
000282474 7001_ $$aSong, Chengyuan$$b3
000282474 7001_ $$aBurns, Ryan$$b4
000282474 7001_ $$0P:(DE-HGF)0$$aKruse, Niels$$b5
000282474 7001_ $$aSantos, Patrícia I$$b6
000282474 7001_ $$0P:(DE-2719)9000670$$aMilovanovic, Dragomir$$b7$$udzne
000282474 7001_ $$0P:(DE-2719)2811373$$aHöglinger, Günter$$b8$$udzne
000282474 7001_ $$0P:(DE-2719)9001340$$aMollenhauer, Brit$$b9$$udzne
000282474 7001_ $$aLuk, Kelvin C$$b10
000282474 7001_ $$aLee, Virginia My-$$b11
000282474 7001_ $$0P:(DE-2719)2814138$$aOuteiro, Tiago F$$b12$$udzne
000282474 773__ $$0PERI:(DE-600)2819218-7$$a10.1038/s41531-025-01144-3$$gVol. 11, no. 1, p. 326$$n1$$p326$$tnpj Parkinson's Disease$$v11$$x2373-8057$$y2025
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