Year: 2025
Type: article
Abstract: The SWI/SNF family complexes are highly conserved across evolution, and play a critical role in regulation of gene expression. The SWI/SNF homologs in mammalian cells (mSWI/SNF) are often referred to as the Brg1-asscoiated factor (BAF) complexes. In line with their broad functionality, mutations of the BAF complexes are found in over 20% of human cancers 1 , whereas accumulating evidence indicates that the intact complexes are required for tumorigenesis of many cancer types 2 . The BAF complexes are assembled into three major forms: canonical BAF (cBAF), Poly-bromo associated BAF (PBAF), and non-canonical BAF (ncBAF). Different from cBAF and PBAF, ncBAF lacks the essential nucleosome-binding subunit SMARCB1 and the scaffold subunit (ARID1A in cBAF or ARID2 in PBAF) 3 . While the structures of cBAF and PBAF bound to the nucleosome were determined 4 , 5 , 6 , 7 , how the ncBAF complex interacts with the nucleosome substrate remains unknown. Here we report the cryo-electron microscopy (cryo-EM) structure of the human ncBAF complex bound to the nucleosome, revealing the unique mechanism of nucleosome recognition by ncBAF.
Source: Cell Discovery
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,590
OpenAlex ID: W4417368886