Thanks a lot!

Thanks a lot Ariel. We hope it may increase focus on IDR-domain interactions, we think there’s a lot to do in that space. Hope you’re doing great!

Thank you so much!

We were very lucky to have so many amazing collaborators on this paper, including @vaclav-veverka.bsky.social, @cermakova.bsky.social, and many others, including Yuen San Chan as first author. Please check out our paper for more information!

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

We also show that neural crest cells and NCC-derived neurons tolerate SWI/SNF inhibition. I anticipate that non-cycling cells are frequently independent, and cycling cells with different circuitries have alternatives or plasticity to activate Cyclin D

Thanks Hiten, it is surprising that SWI/SNF inhibition is well tolerated, and we've seen very good therapeutic window in vivo. Not all cycling cells need SWI/SNF, it's dispensable for example in HEK293Ts