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Molecular chaperones play important roles in protein misfolding diseases and members of the chaperone machinery are often deposited in Lewy bodies. Here, we show that the Hsp90 co-chaperone STI1 co-immunoprecipitated \u03b1-synuclein, and co-deposited with Hsp90 and Hsp70 in insoluble protein fractions in two mouse models of \u03b1-synuclein misfolding. STI1 and Hsp90 also co-localized extensively with filamentous S129 phosphorylated \u03b1-synuclein in ubiquitin-positive inclusions. In PD human brains, STI1 transcripts were increased, and in neurologically healthy brains, STI1 and \u03b1-synuclein transcripts correlated. Nuclear Magnetic Resonance (NMR) analyses revealed direct interaction of \u03b1-synuclein with STI1 and indicated that the STI1 TPR2A, but not TPR1 or TPR2B domains, interacted with the C-terminal domain of \u03b1-synuclein. In vitro, the STI1 TPR2A domain facilitated S129 phosphorylation by Polo-like kinase 3. Moreover, mice over-expressing STI1 and Hsp90\u00df presented elevated \u03b1-synuclein S129 phosphorylation accompanied by inclusions when injected with \u03b1-synuclein pre-formed fibrils. In contrast, reduced STI1 function decreased protein inclusion formation, S129 \u03b1-synuclein phosphorylation, while mitigating motor and cognitive deficits as well as mesoscopic brain atrophy in \u03b1-synuclein-over-expressing mice. Our findings reveal a vicious cycle in which STI1 facilitates the generation and accumulation of toxic \u03b1-synuclein conformers, while \u03b1-synuclein-induced proteostatic stress increased insoluble STI1 and Hsp90.<\/jats:p>","DOI":"10.1007\/s00401-022-02491-8","type":"journal-article","created":{"date-parts":[[2022,9,19]],"date-time":"2022-09-19T08:02:45Z","timestamp":1663574565000},"page":"881-910","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":31,"title":["Stress-inducible phosphoprotein 1 (HOP\/STI1\/STIP1) regulates the accumulation and toxicity of \u03b1-synuclein in vivo"],"prefix":"10.1007","volume":"144","author":[{"given":"Rachel E.","family":"Lackie","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aline S.","family":"de Miranda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mei Peng","family":"Lim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladislav","family":"Novikov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nimrod","family":"Madrer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nadun C.","family":"Karunatilleke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin S.","family":"Rutledge","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephanie","family":"Tullo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anne","family":"Brickenden","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew E. 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Cambridge Enterprise, the technology transfer office of the University of Cambridge, supported commercialization of the Bussey\u2013Saksida chamber, culminating in a license to Campden Instruments. Any financial compensation received from commercialization of the technology is fully invested in further touchscreen development and\/or maintenance.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}