Excitingly, β-catenin links cBAF not only to SF-1, but also to YAP1, SOX2, FOXO3, and CBP/p300, highlighting its critical role in chromatin remodeling across diverse cellular processes

Dissection of interactions revealed that intrinsically disordered regions (IDRs) of ARID1A bind directly to the structured Armadillo domain of β-catenin

Sustained inhibition leads to loss of steroid production, positioning cBAF as a key steroidogenic dependency

We show that BAF inhibition disrupts the ability of the TF known as steroidogenic factor 1 (SF-1) and β-catenin to bind at enhancers targeted by ARID1A

How do chromatin remodelers use #IDRs to find TF binding partners? In our new Molecular Cell paper, we show that β-catenin is an adaptor that links SWI/SNF (cBAF) subunit ARID1A with binding partners via IDR-domain interactions.
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