Rapid and reversible dissolution of biomolecular condensates using light-controlled recruitment of a solubility tag

Ellen H. Brumbaugh-Reed, Yang Gao, Kazuhiro Aoki and Jared E. Toettcher ()
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Ellen H. Brumbaugh-Reed: Princeton University
Yang Gao: Princeton University
Kazuhiro Aoki: National Institutes of Natural Sciences
Jared E. Toettcher: Princeton University

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Biomolecular condensates are broadly implicated in both normal cellular regulation and disease. Consequently, several chemical biology and optogenetic approaches have been developed to induce phase separation of a protein of interest. However, few tools are available to perform the converse function – dissolving a condensate of interest on demand. Such a tool would aid in testing whether the condensate plays specific functional roles. Here we show that light-gated recruitment of a solubilizing domain, maltose-binding protein (MBP), results in rapid and controlled dissolution of condensates formed from proteins of interest. Our optogenetic MBP-based dissolution strategy (OptoMBP) is rapid, reversible, and can be spatially controlled with subcellular precision. We also provide a proof-of-principle application of OptoMBP by disrupting condensation of the oncogenic fusion protein FUS-CHOP and reverting FUS-CHOP driven transcriptional changes. We envision that the OptoMBP system could be broadly useful for disrupting constitutive protein condensates to probe their biological functions.

Date: 2024
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DOI: 10.1038/s41467-024-50858-0

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