Heterotypic interactions can drive selective co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex

Richoo B. Davis, Anushka Supakar, Aishwarya Kanchi Ranganath, Mahdi Muhammad Moosa and Priya R. Banerjee ()
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Richoo B. Davis: University at Buffalo
Anushka Supakar: University at Buffalo
Aishwarya Kanchi Ranganath: University at Buffalo
Mahdi Muhammad Moosa: University at Buffalo
Priya R. Banerjee: University at Buffalo

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract Prion-like domains (PLDs) are low-complexity protein sequences enriched within nucleic acid-binding proteins including those involved in transcription and RNA processing. PLDs of FUS and EWSR1 play key roles in recruiting chromatin remodeler mammalian SWI/SNF (mSWI/SNF) complex to oncogenic FET fusion protein condensates. Here, we show that disordered low-complexity domains of multiple SWI/SNF subunits are prion-like with a strong propensity to undergo intracellular phase separation. These PLDs engage in sequence-specific heterotypic interactions with the PLD of FUS in the dilute phase at sub-saturation conditions, leading to the formation of PLD co-condensates. In the dense phase, homotypic and heterotypic PLD interactions are highly cooperative, resulting in the co-mixing of individual PLD phases and forming spatially homogeneous condensates. Heterotypic PLD-mediated positive cooperativity in protein-protein interaction networks is likely to play key roles in the co-phase separation of mSWI/SNF complex with transcription factors containing homologous low-complexity domains.

Date: 2024
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DOI: 10.1038/s41467-024-44945-5

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