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Here, we report that upon impairments in mitochondrial protein import, high-risk precursor and immature forms of mitochondrial proteins form aberrant deposits in the cytosol. These deposits then cause further cytosolic accumulation and consequently aggregation of other mitochondrial proteins and disease-related proteins, including \u03b1-synuclein and amyloid \u03b2. This aggregation triggers a cytosolic protein homeostasis imbalance that is accompanied by specific molecular chaperone responses at both the transcriptomic and protein levels. Altogether, our results provide evidence that mitochondrial dysfunction, specifically protein import defects, contributes to impairments in protein homeostasis, thus revealing a possible molecular mechanism by which mitochondria are involved in neurodegenerative diseases.<\/jats:p>","DOI":"10.7554\/elife.65484","type":"journal-article","created":{"date-parts":[[2021,7,20]],"date-time":"2021-07-20T09:00:11Z","timestamp":1626771611000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.65484","source":"Crossref","is-referenced-by-count":107,"title":["Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins"],"prefix":"10.7554","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7446-3786","authenticated-orcid":true,"given":"Urszula","family":"Nowicka","sequence":"first","affiliation":[{"name":"ReMedy International Research Agenda Unit, University of Warsaw","place":["Warsaw, Poland"]},{"name":"Centre of 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