Researchers from Brown University and Hasbro Children’s Hospital have identified the molecular interactions that allow the protein survivin to leave the nucleus of a breast cancer cell, prolonging the cell’s life. They discovered how the proteins HDAC6, CBP, and CRM1 aid survivin in its escape. HDAC6 gathers at the boundary between the nucleus and the rest of the cell, and then becomes activated by CBP, which chemically regulates survivin under normal circumstances. The HDAC6 then undoes the process used to regulate survivin, called acetylation, allowing the protein to be shuttled out of the nucleus by CRM1. This discovery could lead to new approaches to treating breast cancer, such as inhibiting HDAC6. “If we can target HDAC6, we can maybe block survivin from coming out of the nucleus and maintain it in its good state,” Rachel Altura, the study’s senior author, said.