Structure and molecular function of the BCL7 proteins

Initially identified through chromosomal translocations in lymphomas, the BCL7 protein family, comprising the three paralogues BCL7A, BCL7B, and BCL7C, has recently emerged as a core component of mammalian SWI/SNF ATP-dependent chromatin remodeling complexes. Although their functions remained poorly understood for many years, recent structural and biochemical studies have substantially improved our understanding of their roles. Cryo-electron microscopy studies revealed that BCL7 proteins interact with nucleosomes through a conserved N-terminal arginine anchor motif that binds the nucleosomal acidic patch and stabilize the actin-related protein module through a conserved β-hairpin motif. These findings identify BCL7 proteins as structural elements that contribute to nucleosome engagement and SWI/SNF complex integrity. Comparative analyses further suggest that key structural features of BCL7 proteins are conserved across evolution despite limited sequence similarity. In addition to their roles in chromatin remodeling, increasing evidence links BCL7 proteins to hematological malignancies, solid tumors, and developmental disorders, highlighting their emerging value as biomarkers and potential therapeutic targets. This review summarizes current knowledge on the structure, evolution, and functions of the BCL7 family and outlines future directions for elucidating their contribution to chromatin regulation and disease.