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The mechanisms that govern the liquid-to-solid phase transition of TDP-43 remain poorly defined. Here, we combined chemical and genome-wide genetic screens to identify cellular factors that modulate the phase behavior of an RNA-binding-defective TDP-43 mutant. Our screens uncovered multiple cellular processes, including RNA splicing, protein translation, proteostasis imbalance, and nuclear export as TDP-43 phase regulators. We also developed a semi-permeabilized cell system that partially recapitulates the TDP-43 phase transition in vitro, and showed that nuclear export inhibition reshapes the nuclear environment to favor RNA-dependent liquid-liquid phase separation (LLPS) of TDP-43, which mitigates its aggregation. Nuclear export inhibition in a brain organoid model bearing an ALS-associated mutation reduces pathogenic phospho-TDP-43 accumulation. These findings identify multiple modulators of TDP-43 phase transitions in a sensitized model system and establish a framework for further dissecting the link between nuclear transport and TDP-43 phase dynamics.<\/jats:p>","DOI":"10.7554\/elife.110172","type":"journal-article","created":{"date-parts":[[2026,3,2]],"date-time":"2026-03-02T14:30:18Z","timestamp":1772461818000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.110172","source":"Crossref","is-referenced-by-count":0,"title":["Cellular modifiers of TDP-43 phase transition and cytoplasmic aggregation"],"prefix":"10.7554","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-6370-730X","authenticated-orcid":true,"given":"Natalie","family":"Chin","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00adh9b73","id-type":"ROR","asserted-by":"publisher"}],"name":"Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of 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